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6et5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Reaction centre light harvesting complex 1 from Blc. virids== | |
| + | <SX load='6et5' size='340' side='right' viewer='molstar' caption='[[6et5]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6et5]] is a 54 chain structure with sequence from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ET5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ET5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=NS0:all-trans-1,2-dihydroneurosporene'>NS0</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ9:UBIQUINONE-9'>UQ9</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</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=6et5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6et5 OCA], [http://pdbe.org/6et5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6et5 RCSB], [http://www.ebi.ac.uk/pdbsum/6et5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6et5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LHB_BLAVI LHB_BLAVI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. [[http://www.uniprot.org/uniprot/RCEH_BLAVI RCEH_BLAVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/CYCR_BLAVI CYCR_BLAVI]] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.<ref>PMID:10736158</ref> [[http://www.uniprot.org/uniprot/RCEM_BLAVI RCEM_BLAVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/LHG_BLAVI LHG_BLAVI]] One of the components of the bacteriochlorophyll-protein complex in the chromatophore membrane. [[http://www.uniprot.org/uniprot/RCEL_BLAVI RCEL_BLAVI]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/LHA_BLAVI LHA_BLAVI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The light-harvesting 1-reaction centre (LH1-RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 A resolution cryo-electron microscopy structure of the bacteriochlorophyll b-based LH1-RC complex from Blastochloris viridis that reveals the structural basis for absorption of infrared light and the molecular mechanism of quinone migration across the LH1 complex. The triple-ring LH1 complex comprises a circular array of 17 beta-polypeptides sandwiched between 17 alpha- and 16 gamma-polypeptides. Tight packing of the gamma-apoproteins between beta-polypeptides collectively interlocks and stabilizes the LH1 structure; this, together with the short Mg-Mg distances of bacteriochlorophyll b pairs, contributes to the large redshift of bacteriochlorophyll b absorption. The 'missing' 17th gamma-polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a quinone, Q P, which adopts a compact, export-ready conformation before passage through the pore and eventual diffusion to the cytochrome bc 1 complex. | ||
| - | + | Cryo-EM structure of the Blastochloris viridis LH1-RC complex at 2.9 A.,Qian P, Siebert CA, Wang P, Canniffe DP, Hunter CN Nature. 2018 Apr;556(7700):203-208. doi: 10.1038/s41586-018-0014-5. Epub 2018 Apr, 4. PMID:29618818<ref>PMID:29618818</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6et5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Blastochloris viridis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Canniffe, D P]] | ||
| + | [[Category: Hunter, C N]] | ||
| + | [[Category: Qian, P]] | ||
| + | [[Category: Siebert, C A]] | ||
| + | [[Category: Wang, P]] | ||
| + | [[Category: Photosynthesis]] | ||
| + | [[Category: Reaction centre light harvesting complex 1 blc. viridis cryo-em rc-lh1 photosynthesis]] | ||
Current revision
Reaction centre light harvesting complex 1 from Blc. virids
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