View source for 6f0k


==Alternative complex III==
<SX load='6f0k' size='340' side='right' viewer='molstar' caption='[[6f0k]], [[Resolution|resolution]] 3.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6f0k]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus_DSM_4252 Rhodothermus marinus DSM 4252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F0K 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]] 3.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=6f0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0k OCA], [https://pdbe.org/6f0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f0k RCSB], [https://www.ebi.ac.uk/pdbsum/6f0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D0MDD4_RHOM4 D0MDD4_RHOM4] 
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== Publication Abstract from PubMed ==
Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 A resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.

Structural basis for energy transduction by respiratory alternative complex III.,Sousa JS, Calisto F, Langer JD, Mills DJ, Refojo PN, Teixeira M, Kuhlbrandt W, Vonck J, Pereira MM Nat Commun. 2018 Apr 30;9(1):1728. doi: 10.1038/s41467-018-04141-8. PMID:29712914<ref>PMID:29712914</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6f0k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Rhodothermus marinus DSM 4252]]
[[Category: Calisto F]]
[[Category: Kuehlbrandt W]]
[[Category: Mills DJ]]
[[Category: Pereira MM]]
[[Category: Sousa JS]]
[[Category: Vonck J]]