5l8r

From Proteopedia

(Difference between revisions)

Revision as of 16:11, 4 October 2023

The structure of plant photosystem I super-complex at 2.6 angstrom resolution.

Structural highlights

5l8r is a 10 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	, , , , , , , , , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

E1C9L2_PEA May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.[ARBA:ARBA00003702] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.[RuleBase:RU363080]

Publication Abstract from PubMed

Four elaborate membrane complexes carry out the light reaction of oxygenic photosynthesis. Photosystem I (PSI) is one of two large reaction centres responsible for converting light photons into the chemical energy needed to sustain life. In the thylakoid membranes of plants, PSI is found together with its integral light-harvesting antenna, light-harvesting complex I (LHCI), in a membrane supercomplex containing hundreds of light-harvesting pigments. Here, we report the crystal structure of plant PSI-LHCI at 2.6 A resolution. The structure reveals the configuration of PsaK, a core subunit important for state transitions in plants, a conserved network of water molecules surrounding the electron transfer centres and an elaborate structure of lipids bridging PSI and its LHCI antenna. We discuss the implications of the structure for energy transfer and the evolution of PSI.

Structure of the plant photosystem I supercomplex at 2.6 A resolution.,Mazor Y, Borovikova A, Caspy I, Nelson N Nat Plants. 2017 Mar 1;3:17014. doi: 10.1038/nplants.2017.14. PMID:28248295^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mazor Y, Borovikova A, Caspy I, Nelson N. Structure of the plant photosystem I supercomplex at 2.6 A resolution. Nat Plants. 2017 Mar 1;3:17014. doi: 10.1038/nplants.2017.14. PMID:28248295 doi:http://dx.doi.org/10.1038/nplants.2017.14

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5l8r"

@@ Line 3: / Line 3: @@
 <StructureSection load='5l8r' size='340' side='right'caption='[[5l8r]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5l8r]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L8R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5l8r]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L8R 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CHL:CHLOROPHYLL+B'>CHL</scene>, <scene name='pdbligand=CL0:CHLOROPHYLL+A+ISOMER'>CL0</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=LUT:(3R,3R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>LUT</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XAT:(3S,5R,6S,3S,5R,6S)-5,6,5,6-DIEPOXY-5,6,5,6-+TETRAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>XAT</scene>, <scene name='pdbligand=ZEX:(3S,5R,6S,3S,5R,6S)+BETA-CAROTENE-3,23-DIOL'>ZEX</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]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y28|4y28]], [[1jb0|1jb0]], [[4xk8|4xk8]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CHL:CHLOROPHYLL+B'>CHL</scene>, <scene name='pdbligand=CL0:CHLOROPHYLL+A+ISOMER'>CL0</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=LUT:(3R,3R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>LUT</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XAT:(3S,5R,6S,3S,5R,6S)-5,6,5,6-DIEPOXY-5,6,5,6-+TETRAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>XAT</scene>, <scene name='pdbligand=ZEX:(3S,5R,6S,3S,5R,6S)+BETA-CAROTENE-3,23-DIOL'>ZEX</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Photosystem_I Photosystem I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.97.1.12 1.97.1.12] </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=5l8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8r OCA], [https://pdbe.org/5l8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l8r RCSB], [https://www.ebi.ac.uk/pdbsum/5l8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8r ProSAT]</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=5l8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l8r OCA], [http://pdbe.org/5l8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l8r RCSB], [http://www.ebi.ac.uk/pdbsum/5l8r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l8r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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/A0A0F6NGI2_PEA A0A0F6NGI2_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.[HAMAP-Rule:MF_00482] [[http://www.uniprot.org/uniprot/CB23_PEA CB23_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/D5MAL3_PEA D5MAL3_PEA]] May help in the organization of the PsaE and PsaF subunits.[HAMAP-Rule:MF_00522] [[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/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/E1C9L2_PEA E1C9L2_PEA] May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.[ARBA:ARBA00003702]  The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.[RuleBase:RU363080]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 ==See Also==
-*[[Photosystem I|Photosystem I]]
+*[[Photosystem I 3D structures|Photosystem I 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Photosystem I]]
 [[Category: Pisum sativum]]
-[[Category: Borovikova, A]]
+[[Category: Borovikova A]]
-[[Category: Caspy, I]]
+[[Category: Caspy I]]
-[[Category: Mazor, Y]]
+[[Category: Mazor Y]]
-[[Category: Nelson, N]]
+[[Category: Nelson N]]
-[[Category: Chlorophyll]]
-[[Category: Light harvesting]]
-[[Category: Membrane complex]]
-[[Category: Oxidoreductase]]
-[[Category: Photosynthesis]]

5l8r

From Proteopedia

Revision as of 16:11, 4 October 2023

The structure of plant photosystem I super-complex at 2.6 angstrom resolution.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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