2o01 - Revision history

OCA at 10:28, 30 August 2023

OCA — Wed, 30 Aug 2023 10:28:11 GMT

←Older revision		Revision as of 10:28, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='2o01' size='340' side='right'caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='2o01' size='340' side='right'caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana~~], [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris~~], [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O01 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2o01]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O01 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BCR:BETA~~-~~CAROTENE'>BCR</scene>~~, ~~<scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.4Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~UNK~~:~~UNKNOWN~~'>~~UNK~~</scene><~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<~~tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max-height: 3em;~~'>~~[[1qzv\|1qzv]]~~</~~div~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [https://pdbe.org/2o01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [https://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [https://pdbe.org/2o01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [https://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[https://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[https://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[https://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[https://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[https://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[https://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[https://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[https://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[https://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[https://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).	+	[https://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 31:

	==See Also==		==See Also==
-	*[[Photosystem I\|Photosystem I]]	+	*[[Photosystem I 3D structures\|Photosystem I 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 38:
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Phaseolus vulgaris]]
	[[Category: Pisum sativum]]		[[Category: Pisum sativum]]
	[[Category: Spinacia oleracea]]		[[Category: Spinacia oleracea]]
-	[[Category: Amunts, A]]	+	[[Category: Amunts A]]
-	[[Category: Drory, O]]	+	[[Category: Drory O]]
-	[[Category: Nelson, N]]	+	[[Category: Nelson N]]
-	~~[[Category: Membranal super complex]]~~	+
-	~~[[Category: Photosynthesis~~]]	+

OCA at 09:08, 23 February 2022

OCA — Wed, 23 Feb 2022 09:08:24 GMT

←Older revision		Revision as of 09:08, 23 February 2022
Line 3:		Line 3:
	<StructureSection load='2o01' size='340' side='right'caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='2o01' size='340' side='right'caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [~~http~~://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [~~http~~://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [~~http~~://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2O01 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O01 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qzv\|1qzv]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [~~http~~://pdbe.org/2o01 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [https://pdbe.org/2o01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [https://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[~~http~~://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[~~http~~://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[~~http~~://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[~~http~~://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[~~http~~://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[~~http~~://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[~~http~~://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[~~http~~://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[~~http~~://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[~~http~~://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).	+	[[https://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[https://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[https://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[https://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[https://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[https://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[https://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[https://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[https://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[https://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[https://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:36, 20 May 2020

OCA — Wed, 20 May 2020 06:36:48 GMT

←Older revision		Revision as of 06:36, 20 May 2020
Line 1:		Line 1:

	==The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution==		==The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution==
-	<StructureSection load='2o01' size='340' side='right' caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>	+	<StructureSection load='2o01' size='340' side='right'caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2O01 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2O01 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://pdbe.org/2o01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://pdbe.org/2o01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~CB24_PEA CB24_PEA~~]] ~~The light-harvesting complex~~ (~~LHC~~) ~~functions as a light receptor, it captures and delivers excitation energy~~ to ~~photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in~~ the ~~catalytic Mn center~~ of ~~water oxidation into the thylakoid lumen~~.~~<ref>PMID:2174365</ref>~~ [[http://www.uniprot.org/uniprot/~~PSAB_PEA PSAB_PEA~~]] ~~PsaA and PsaB bind P700,~~ the ~~primary electron donor~~ of photosystem I (PSI)~~, as well as~~ the electron ~~acceptors A0~~, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn~~. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin~~ (By similarity). [[http://www.uniprot.org/uniprot/~~PSAA_PEA PSAA_PEA~~]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin~~. [[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700~~ (~~or cytochrome c553 in algae and cyanobacteria~~)~~. This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI~~. [[http://www.uniprot.org/uniprot/~~PSAC_PEA PSAC_PEA~~]] ~~Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin.~~ The C-~~terminus interacts with PsaA/B/D and helps assemble the protein into the PSI~~ complex~~. Required for binding of PsaD and PsaE to PSI. PSI is~~ a ~~plastocyanin-ferredoxin oxidoreductase~~, ~~converting photonic~~ excitation ~~into a charge separation,~~ which ~~transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity)~~.~~[HAMAP-Rule:MF_01303] [[http~~:/~~/www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]]~~ May ~~help~~ in the ~~organization~~ of the ~~PsaL subunit~~. [[http://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).	+	[[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[http://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[http://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[http://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
		+	[[Category: Large Structures]]
	[[Category: Phaseolus vulgaris]]		[[Category: Phaseolus vulgaris]]
	[[Category: Pisum sativum]]		[[Category: Pisum sativum]]

OCA at 16:48, 15 August 2018

OCA — Wed, 15 Aug 2018 16:48:45 GMT

←Older revision		Revision as of 16:48, 15 August 2018
Line 1:		Line 1:
		+
	==The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution==		==The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution==
	<StructureSection load='2o01' size='340' side='right' caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='2o01' size='340' side='right' caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://pdbe.org/2o01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://pdbe.org/2o01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o01 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~PSAF_SPIOL PSAF_SPIOL~~]] ~~Probably participates in efficiency of electron transfer from plastocyanin to P700~~ (~~or cytochrome c553 in algae and cyanobacteria~~)~~. This plastocyanin-docking protein contributes~~ to the ~~specific association~~ of ~~plastocyanin to PSI~~. [[http://www.uniprot.org/uniprot/~~PSAC_PEA PSAC_PEA~~]] ~~Apoprotein for the two 4Fe-4S centers FA~~ and FB of photosystem I (PSI)~~; essential for photochemical activity. FB is~~ the ~~terminal~~ electron ~~acceptor of PSI~~, ~~donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D~~ and ~~helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI~~. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).~~[HAMAP-Rule:MF_01303]~~ [[http://www.uniprot.org/uniprot/~~PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA~~]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (~~By similarity~~). [[http://www.uniprot.org/uniprot/~~CB24_PEA CB24_PEA~~]] ~~The light~~-~~harvesting complex~~ (~~LHC~~) ~~functions as a light receptor~~, ~~it captures and delivers excitation energy~~ to ~~photosystems~~ with ~~which it~~ is ~~closely associated~~.~~<ref>PMID~~:~~2174365<~~/~~ref>~~ May ~~channel protons produced~~ in the ~~catalytic Mn center~~ of ~~water oxidation into~~ the ~~thylakoid lumen~~.~~<ref>PMID:2174365</ref>~~ [[http://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).	+	[[http://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[http://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/2o01_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/2o01_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o01 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 14:15, 11 September 2015

OCA — Fri, 11 Sep 2015 14:15:19 GMT

←Older revision		Revision as of 14:15, 11 September 2015
Line 6:		Line 6:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://pdbe.org/2o01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[http://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).	+	[[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[http://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[http://www.uniprot.org/uniprot/CB24_PEA CB24_PEA]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.<ref>PMID:2174365</ref> May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.<ref>PMID:2174365</ref> [[http://www.uniprot.org/uniprot/CAB6_ARATH CAB6_ARATH]] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2o01" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:34, 25 December 2014

OCA — Thu, 25 Dec 2014 17:34:42 GMT

←Older revision		Revision as of 17:34, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O01 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O01 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PSAF_SPIOL PSAF_SPIOL]] Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. [[http://www.uniprot.org/uniprot/PSAC_PEA PSAC_PEA]] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_PEA PSAI_PEA]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB_PEA PSAB_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin (By similarity). [[http://www.uniprot.org/uniprot/PSAH_SPIOL PSAH_SPIOL]] Possible role could be the docking of the LHC I antenna complex to the core complex. [[http://www.uniprot.org/uniprot/PSAD_SPIOL PSAD_SPIOL]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein. [[http://www.uniprot.org/uniprot/PSAA_PEA PSAA_PEA]] PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. [[http://www.uniprot.org/uniprot/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAE1_ARATH PSAE1_ARATH]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 39:
	[[Category: Pisum sativum]]		[[Category: Pisum sativum]]
	[[Category: Spinacia oleracea]]		[[Category: Spinacia oleracea]]
-	[[Category: Amunts, A.]]	+	[[Category: Amunts, A]]
-	[[Category: Drory, O.]]	+	[[Category: Drory, O]]
-	[[Category: Nelson, N.]]	+	[[Category: Nelson, N]]
	[[Category: Membranal super complex]]		[[Category: Membranal super complex]]
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]

OCA at 04:57, 29 September 2014

OCA — Mon, 29 Sep 2014 04:57:12 GMT

←Older revision		Revision as of 04:57, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2o01.~~png~~\|~~left~~\|200px]]	+	==The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution==
		+	<StructureSection load='2o01' size='340' side='right' caption='[[2o01]], [[Resolution\|resolution]] 3.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O01 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qzv\|1qzv]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o01 RCSB], [http://www.ebi.ac.uk/pdbsum/2o01 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/2o01_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	All higher organisms on Earth receive energy directly or indirectly from oxygenic photosynthesis performed by plants, green algae and cyanobacteria. Photosystem I (PSI) is a supercomplex of a reaction centre and light-harvesting complexes. It generates the most negative redox potential in nature, and thus largely determines the global amount of enthalpy in living systems. We report the structure of plant PSI at 3.4 A resolution, revealing 17 protein subunits. PsaN was identified in the luminal side of the supercomplex, and most of the amino acids in the reaction centre were traced. The crystal structure of PSI provides a picture at near atomic detail of 11 out of 12 protein subunits of the reaction centre. At this level, 168 chlorophylls (65 assigned with orientations for Q(x) and Q(y) transition dipole moments), 2 phylloquinones, 3 Fe(4)S(4) clusters and 5 carotenoids are described. This structural information extends the understanding of the most efficient nano-photochemical machine in nature.

-	~~{{STRUCTURE_2o01\| PDB=2o01 \| SCENE= }}~~	+	The structure of a plant photosystem I supercomplex at 3.4 A resolution.,Amunts A, Drory O, Nelson N Nature. 2007 May 3;447(7140):58-63. PMID:17476261<ref>PMID:17476261</ref>

-	~~===The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17476261}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki~~/~~Arabidopsis_thaliana Arabidopsis thaliana]~~, ~~[http://en~~.~~wikipedia~~.~~org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en~~.~~wikipedia.org~~/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA].	+

	==See Also==		==See Also==
	*[[Photosystem I\|Photosystem I]]		*[[Photosystem I\|Photosystem I]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017476261<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Phaseolus vulgaris]]		[[Category: Phaseolus vulgaris]]

OCA at 19:31, 20 October 2012

OCA — Sat, 20 Oct 2012 19:31:01 GMT

←Older revision		Revision as of 19:31, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2o01]] is a 17 chain structure ~~of [[Photosystem I]]~~ with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA].	+	[[2o01]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA].

	==See Also==		==See Also==

OCA: Protected "2o01" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 06:00:20 GMT

Protected "2o01" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:00, 25 July 2012

OCA at 06:00, 25 July 2012

OCA — Wed, 25 Jul 2012 06:00:19 GMT

←Older revision		Revision as of 06:00, 25 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2o01.png\|left\|200px]]		[[Image:2o01.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2o01", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2o01\| PDB=2o01 \| SCENE= }}		{{STRUCTURE_2o01\| PDB=2o01 \| SCENE= }}

	===The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution===		===The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17476261}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17476261 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17476261}}		{{ABSTRACT_PUBMED_17476261}}

	==About this Structure==		==About this Structure==
-	~~2O01~~ is a 17 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA].	+	[[2o01]] is a 17 chain structure of [[Photosystem I]] with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris], [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O01 OCA].
		+
		+	==See Also==
		+	*[[Photosystem I\|Photosystem I]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17476261~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017476261</ref><references group="xtra"/>
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Phaseolus vulgaris]]		[[Category: Phaseolus vulgaris]]
Line 33:		Line 24:
	[[Category: Membranal super complex]]		[[Category: Membranal super complex]]
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:21:26 2009''