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| | <StructureSection load='2wse' size='340' side='right'caption='[[2wse]], [[Resolution|resolution]] 3.49Å' scene=''> | | <StructureSection load='2wse' size='340' side='right'caption='[[2wse]], [[Resolution|resolution]] 3.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wse]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [http://en.wikipedia.org/wiki/Glycine_max Glycine max], [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare], [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=2WSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WSE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wse]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare], [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=2WSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WSE 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=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 3.49Å</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=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wsc|2wsc]], [[2wsf|2wsf]]</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=2wse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wse OCA], [https://pdbe.org/2wse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wse RCSB], [https://www.ebi.ac.uk/pdbsum/2wse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wse 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=2wse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wse OCA], [http://pdbe.org/2wse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wse RCSB], [http://www.ebi.ac.uk/pdbsum/2wse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wse ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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/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/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/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/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/PSAJ_SPIOL PSAJ_SPIOL]] May help in the organization of the PsaE and PsaF subunits. [[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/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/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/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/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]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/2wse_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/2wse_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Photosystem I|Photosystem I]] | + | *[[Photosystem I 3D structures|Photosystem I 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Glycine max]] | |
| | [[Category: Hordeum vulgare]] | | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
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| | [[Category: Pisum sativum]] | | [[Category: Pisum sativum]] |
| | [[Category: Spinacia oleracea]] | | [[Category: Spinacia oleracea]] |
| - | [[Category: Amunts, A]] | + | [[Category: Amunts A]] |
| - | [[Category: Borovikov, A]] | + | [[Category: Borovikov A]] |
| - | [[Category: Nelson, N]] | + | [[Category: Nelson N]] |
| - | [[Category: Toporik, H]] | + | [[Category: Toporik H]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Large complex]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
2wse is a 10 chain structure with sequence from Arabidopsis thaliana, Hordeum vulgare, Phaseolus vulgaris, Pisum sativum and Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 3.49Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Photosystem I functions as a sunlight energy converter, catalyzing one of the initial steps in driving oxygenic photosynthesis in cyanobacteria, algae, and higher plants. Functionally, Photosystem I captures sunlight and transfers the excitation energy through an intricate and precisely organized antenna system, consisting of a pigment network, to the center of the molecule, where it is used in the transmembrane electron transfer reaction. Our current understanding of the sophisticated mechanisms underlying these processes has profited greatly from elucidation of the crystal structures of the Photosystem I complex. In this report, we describe the developments that ultimately led to enhanced structural information of plant Photosystem I. In addition, we report an improved crystallographic model at 3.3-A resolution, which allows analysis of the structure in more detail. An improved electron density map yielded identification and tracing of subunit PsaK. The location of an additional ten beta-carotenes as well as five chlorophylls and several loop regions, which were previously uninterpretable, are now modeled. This represents the most complete plant Photosystem I structure obtained thus far, revealing the locations of and interactions among 17 protein subunits and 193 non-covalently bound photochemical cofactors. Using the new crystal structure, we examine the network of contacts among the protein subunits from the structural perspective, which provide the basis for elucidating the functional organization of the complex.
Structure determination and improved model of plant photosystem I.,Amunts A, Toporik H, Borovikova A, Nelson N J Biol Chem. 2010 Jan 29;285(5):3478-86. Epub 2009 Nov 18. PMID:19923216[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Amunts A, Toporik H, Borovikova A, Nelson N. Structure determination and improved model of plant photosystem I. J Biol Chem. 2010 Jan 29;285(5):3478-86. Epub 2009 Nov 18. PMID:19923216 doi:10.1074/jbc.M109.072645
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