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8k5o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the RC-LH core comples from Halorhodospira halochloris== | |
| + | <StructureSection load='8k5o' size='340' side='right'caption='[[8k5o]], [[Resolution|resolution]] 2.42Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8k5o]] is a 55 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorhodospira_halochloris Halorhodospira halochloris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8K5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8K5O FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.42Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LZM:Trans-Geranyl+Bacteriochlorophyll+B'>A1LZM</scene>, <scene name='pdbligand=A1LZP:Trans-Geranyl+Bacteriopheophytin+B'>A1LZP</scene>, <scene name='pdbligand=A1LZQ:Trans-Geranyl+8-vinyl-bacteriochlorophyll+B'>A1LZQ</scene>, <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LYC:LYCOPENE'>LYC</scene>, <scene name='pdbligand=MQ8:MENAQUINONE+8'>MQ8</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</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=8k5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8k5o OCA], [https://pdbe.org/8k5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8k5o RCSB], [https://www.ebi.ac.uk/pdbsum/8k5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8k5o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0X8X829_HALHR A0A0X8X829_HALHR] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[ARBA:ARBA00003196][PIRNR:PIRNR000017] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Halorhodospira (Hlr.) halochloris is a triply extremophilic phototrophic purple sulfur bacterium, as it is thermophilic, alkaliphilic, and extremely halophilic. The light-harvesting-reaction center (LH1-RC) core complex of this bacterium displays an LH1-Q(y) transition at 1,016 nm, which is the lowest-energy wavelength absorption among all known phototrophs. Here we report the cryo-EM structure of the LH1-RC at 2.42 A resolution. The LH1 complex forms a tricyclic ring structure composed of 16 alphabetagamma-polypeptides and one alphabeta-heterodimer around the RC. From the cryo-EM density map, two previously unrecognized integral membrane proteins, referred to as protein G and protein Q, were identified. Both of these proteins are single transmembrane-spanning helices located between the LH1 ring and the RC L-subunit and are absent from the LH1-RC complexes of all other purple bacteria of which the structures have been determined so far. Besides bacteriochlorophyll b molecules (B1020) located on the periplasmic side of the Hlr. halochloris membrane, there are also two arrays of bacteriochlorophyll b molecules (B800 and B820) located on the cytoplasmic side. Only a single copy of a carotenoid (lycopene) was resolved in the Hlr. halochloris LH1-alpha3beta3 and this was positioned within the complex. The potential quinone channel should be the space between the LH1-alpha3beta3 that accommodates the single lycopene but does not contain a gamma-polypeptide, B800 and B820. Our results provide a structural explanation for the unusual Q(y) red shift and carotenoid absorption in the Hlr. halochloris spectrum and reveal new insights into photosynthetic mechanisms employed by a species that thrives under the harshest conditions of any phototrophic microorganism known. | ||
| - | + | Structural insights into the unusual core photocomplex from a triply extremophilic purple bacterium, Halorhodospira halochloris.,Qi CH, Wang GL, Wang FF, Wang J, Wang XP, Zou MJ, Ma F, Madigan MT, Kimura Y, Wang-Otomo ZY, Yu LJ J Integr Plant Biol. 2024 Feb 27. doi: 10.1111/jipb.13628. PMID:38411333<ref>PMID:38411333</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8k5o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Halorhodospira halochloris]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Qi C-H]] | ||
| + | [[Category: Wang G-L]] | ||
| + | [[Category: Yu L-J]] | ||
Current revision
Cryo-EM structure of the RC-LH core comples from Halorhodospira halochloris
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