View source for 6loe


==Cryo-EM structure of the dithionite-reduced photosynthetic alternative complex III from Roseiflexus castenholzii==
<StructureSection load='6loe' size='340' side='right'caption='[[6loe]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6loe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseiflexus_castenholzii_DSM_13941 Roseiflexus castenholzii DSM 13941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LOE 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EL6:[(2~{S})-2-octadecanoyloxypropyl]+octadecanoate'>EL6</scene>, <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=6loe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6loe OCA], [https://pdbe.org/6loe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6loe RCSB], [https://www.ebi.ac.uk/pdbsum/6loe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6loe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7NJ87_ROSCS A7NJ87_ROSCS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alternative complex III (ACIII) is a multisubunit quinol:electron acceptor oxidoreductase that couples quinol oxidation with transmembrane proton translocation in both the respiratory and photosynthetic electron transport chains of bacteria. The coupling mechanism, however, is poorly understood. Here, we report the cryo-EM structures of air-oxidized and dithionite-reduced ACIII from the photosynthetic bacterium Roseiflexus castenholzii at 3.3- and 3.5-A resolution, respectively. We identified a menaquinol binding pocket and an electron transfer wire comprising six hemes and four iron-sulfur clusters that is capable of transferring electrons to periplasmic acceptors. We detected a proton translocation passage in which three strictly conserved, mid-passage residues are likely essential for coupling the redox-driven proton translocation across the membrane. These results allow us to propose a previously unrecognized coupling mechanism that links the respiratory and photosynthetic functions of ACIII. This study provides a structural basis for further investigation of the energy transformation mechanisms in bacterial photosynthesis and respiration.

Cryo-EM structures of the air-oxidized and dithionite-reduced photosynthetic alternative complex III from Roseiflexus castenholzii.,Shi Y, Xin Y, Wang C, Blankenship RE, Sun F, Xu X Sci Adv. 2020 Jul 29;6(31):eaba2739. doi: 10.1126/sciadv.aba2739. eCollection , 2020 Jul. PMID:32832681<ref>PMID:32832681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6loe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Roseiflexus castenholzii DSM 13941]]
[[Category: Blankenship RE]]
[[Category: Shi Y]]
[[Category: Sun F]]
[[Category: Wang C]]
[[Category: Xin YY]]
[[Category: Xu XL]]