5zf0: Difference between revisions
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==X-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem I== | ==X-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem I== | ||
<StructureSection load='5zf0' size='340' side='right' caption='[[5zf0]], [[Resolution|resolution]] 4.20Å' scene=''> | <StructureSection load='5zf0' size='340' side='right'caption='[[5zf0]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zf0]] is a | <table><tr><td colspan='2'>[[5zf0]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus Thermosynechococcus vestitus] and [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZF0 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=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2Å</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=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zf0 OCA], [https://pdbe.org/5zf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zf0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zf0 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PSAE_THEVB PSAE_THEVB] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. | ||
<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 5zf0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5zf0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Photosystem I 3D structures|Photosystem I 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Thermosynechococcus vestitus]] | |||
[[Category: Thermosynechococcus | [[Category: Thermosynechococcus vestitus BP-1]] | ||
[[Category: Thermosynechococcus | [[Category: Ikegami T]] | ||
[[Category: Ikegami | [[Category: Kubota-Kawai H]] | ||
[[Category: Kubota-Kawai | [[Category: Kurisu G]] | ||
[[Category: Kurisu | [[Category: Mutoh R]] | ||
[[Category: Mutoh | [[Category: Nowaczyk M]] | ||
[[Category: Nowaczyk | [[Category: Roegner M]] | ||
[[Category: Roegner | [[Category: Setif P]] | ||
[[Category: Setif | [[Category: Shinmura K]] | ||
[[Category: Shinmura | [[Category: Tanaka T]] | ||
[[Category: Tanaka | |||
Revision as of 11:52, 22 November 2023
X-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem IX-ray Structure of the Electron Transfer Complex between Ferredoxin and Photosystem I
Structural highlights
FunctionPSAE_THEVB Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. Publication Abstract from PubMedPhotosystem I (PSI), a large protein complex located in the thylakoid membrane, mediates the final step in light-driven electron transfer to the stromal electron carrier protein ferredoxin (Fd). Here, we report the first structural description of the PSI-Fd complex from Thermosynechococcus elongatus. The trimeric PSI complex binds three Fds in a non-equivalent manner. While each is recognized by a PSI protomer in a similar orientation, the distances between Fds and the PSI redox centres differ. Fd binding thus entails loss of the exact three-fold symmetry of the PSI's soluble subunits, inducing structural perturbations which are transferred to the lumen through PsaF. Affinity chromatography and nuclear magnetic resonance analyses of PSI-Fd complexes support the existence of two different Fd-binding states, with one Fd being more tightly bound than the others. We propose a dynamic structural basis for productive complex formation, which supports fast electron transfer between PSI and Fd. X-ray structure of an asymmetrical trimeric ferredoxin-photosystem I complex.,Kubota-Kawai H, Mutoh R, Shinmura K, Setif P, Nowaczyk MM, Rogner M, Ikegami T, Tanaka H, Kurisu G Nat Plants. 2018 Apr;4(4):218-224. doi: 10.1038/s41477-018-0130-0. Epub 2018 Apr , 2. PMID:29610537[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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