7s3d: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==Structure of photosystem I with bound ferredoxin from Synechococcus sp. PCC 7335 acclimated to far-red light== | ||
<StructureSection load='7s3d' size='340' side='right'caption='[[7s3d]]' scene=''> | <StructureSection load='7s3d' size='340' side='right'caption='[[7s3d]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7s3d]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7335 Synechococcus sp. PCC 7335]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S3D FirstGlance]. <br> | ||
</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=7s3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s3d OCA], [https://pdbe.org/7s3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s3d RCSB], [https://www.ebi.ac.uk/pdbsum/7s3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s3d ProSAT]</span></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]] 2.91Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CL0:CHLOROPHYLL+A+ISOMER'>CL0</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=F6C:Chlorophyll+F'>F6C</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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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=7s3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s3d OCA], [https://pdbe.org/7s3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s3d RCSB], [https://www.ebi.ac.uk/pdbsum/7s3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s3d ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B4WFP8_SYNS7 B4WFP8_SYNS7] PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.[ARBA:ARBA00002640][RuleBase:RU368104] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Far-red light photoacclimation exhibited by some cyanobacteria allows these organisms to use the far-red region of the solar spectrum (700-800 nm) for photosynthesis. Part of this process includes the replacement of six photosystem I (PSI) subunits with isoforms that confer the binding of chlorophyll (Chl) f molecules that absorb far-red light (FRL). However, the exact sites at which Chl f molecules are bound are still challenging to determine. To aid in the identification of Chl f-binding sites, we solved the cryo-EM structure of PSI from far-red light-acclimated cells of the cyanobacterium Synechococcus sp. PCC 7335. We identified six sites that bind Chl f with high specificity and three additional sites that are likely to bind Chl f at lower specificity. All of these binding sites are in the core-antenna regions of PSI, and Chl f was not observed among the electron transfer cofactors. This structural analysis also reveals both conserved and nonconserved Chl f-binding sites, the latter of which exemplify the diversity in FRL-PSI among species. We found that the FRL-PSI structure also contains a bound soluble ferredoxin, PetF1, at low occupancy, which suggests that ferredoxin binds less transiently than expected according to the canonical view of ferredoxin-binding to facilitate electron transfer. We suggest that this may result from structural changes in FRL-PSI that occur specifically during FRL photoacclimation. | |||
Structure of a photosystem I-ferredoxin complex from a marine cyanobacterium provides insights into far-red light photoacclimation.,Gisriel CJ, Flesher DA, Shen G, Wang J, Ho MY, Brudvig GW, Bryant DA J Biol Chem. 2022 Jan;298(1):101408. doi: 10.1016/j.jbc.2021.101408. Epub 2021 , Nov 15. PMID:34793839<ref>PMID:34793839</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7s3d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Photosystem I 3D structures|Photosystem I 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synechococcus sp. PCC 7335]] | ||
[[Category: Brudvig GW]] | |||
[[Category: Bryant DA]] | |||
[[Category: Flesher DA]] | |||
[[Category: Gisriel CJ]] | |||
[[Category: Ho M]] | |||
[[Category: Shen G]] | |||
[[Category: Wang J]] | |||
Latest revision as of 05:49, 5 June 2024
Structure of photosystem I with bound ferredoxin from Synechococcus sp. PCC 7335 acclimated to far-red light
| ||||||||||||