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| | <SX load='6jeo' size='340' side='right' viewer='molstar' caption='[[6jeo]], [[Resolution|resolution]] 3.30Å' scene=''> | | <SX load='6jeo' size='340' side='right' viewer='molstar' caption='[[6jeo]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jeo]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp._(strain_pcc_7120_/_sag_25.82_/_utex_2576) Nostoc sp. (strain pcc 7120 / sag 25.82 / utex 2576)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JEO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jeo]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JEO 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=CL0:CHLOROPHYLL+A+ISOMER'>CL0</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</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=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">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</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='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=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene></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=6jeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jeo OCA], [http://pdbe.org/6jeo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jeo RCSB], [http://www.ebi.ac.uk/pdbsum/6jeo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jeo 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=6jeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jeo OCA], [https://pdbe.org/6jeo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jeo RCSB], [https://www.ebi.ac.uk/pdbsum/6jeo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jeo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSAF_NOSS1 PSAF_NOSS1]] 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_NOSS1 PSAC_NOSS1]] 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/cytochrome c6-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.[HAMAP-Rule:MF_01303] [[http://www.uniprot.org/uniprot/PSAI_NOSS1 PSAI_NOSS1]] May help in the organization of the PsaL subunit. [[http://www.uniprot.org/uniprot/PSAB1_NOSS1 PSAB1_NOSS1]] 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/cytochrome c6-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 or cytochrome c6 (By similarity). [[http://www.uniprot.org/uniprot/PSAJ_NOSS1 PSAJ_NOSS1]] May help in the organization of the PsaE and PsaF subunits. [[http://www.uniprot.org/uniprot/PSAA_NOSS1 PSAA_NOSS1]] 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/cytochrome c6-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 or cytochrome c6. [[http://www.uniprot.org/uniprot/PSAD_NOSS1 PSAD_NOSS1]] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. [[http://www.uniprot.org/uniprot/PSAE_NOSS1 PSAE_NOSS1]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. | + | [https://www.uniprot.org/uniprot/PSAA_NOSS1 PSAA_NOSS1] 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/cytochrome c6-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 or cytochrome c6. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6jeo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6jeo" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Photosystem I 3D structures|Photosystem I 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Photosystem I]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Akita, F]] | + | [[Category: Akita F]] |
| - | [[Category: Kato, K]] | + | [[Category: Kato K]] |
| - | [[Category: Miyazaki, N]] | + | [[Category: Miyazaki N]] |
| - | [[Category: Nagao, R]] | + | [[Category: Nagao R]] |
| - | [[Category: Shen, J R]] | + | [[Category: Shen JR]] |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Photosystem]]
| + | |
| Structural highlights
Function
PSAA_NOSS1 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/cytochrome c6-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 or cytochrome c6.
Publication Abstract from PubMed
Photosystem I (PSI) functions to harvest light energy for conversion into chemical energy. The organisation of PSI is variable depending on the species of organism. Here we report the structure of a tetrameric PSI core isolated from a cyanobacterium, Anabaena sp. PCC 7120, analysed by single-particle cryo-electron microscopy (cryo-EM) at 3.3 A resolution. The PSI tetramer has a C2 symmetry and is organised in a dimer of dimers form. The structure reveals interactions at the dimer-dimer interface and the existence of characteristic pigment orientations and inter-pigment distances within the dimer units that are important for unique excitation energy transfer. In particular, characteristic residues of PsaL are identified to be responsible for the formation of the tetramer. Time-resolved fluorescence analyses showed that the PSI tetramer has an enhanced excitation-energy quenching. These structural and spectroscopic findings provide insights into the physiological significance of the PSI tetramer and evolutionary changes of the PSI organisations.
Structure of a cyanobacterial photosystem I tetramer revealed by cryo-electron microscopy.,Kato K, Nagao R, Jiang TY, Ueno Y, Yokono M, Chan SK, Watanabe M, Ikeuchi M, Shen JR, Akimoto S, Miyazaki N, Akita F Nat Commun. 2019 Oct 30;10(1):4929. doi: 10.1038/s41467-019-12942-8. PMID:31666526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kato K, Nagao R, Jiang TY, Ueno Y, Yokono M, Chan SK, Watanabe M, Ikeuchi M, Shen JR, Akimoto S, Miyazaki N, Akita F. Structure of a cyanobacterial photosystem I tetramer revealed by cryo-electron microscopy. Nat Commun. 2019 Oct 30;10(1):4929. doi: 10.1038/s41467-019-12942-8. PMID:31666526 doi:http://dx.doi.org/10.1038/s41467-019-12942-8
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