View source for 6hwh


==Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis==
<SX load='6hwh' size='340' side='right' viewer='molstar' caption='[[6hwh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hwh]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HWH 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</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=6hwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hwh OCA], [https://pdbe.org/6hwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hwh RCSB], [https://www.ebi.ac.uk/pdbsum/6hwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hwh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0R051_MYCS2 A0R051_MYCS2] 
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== Publication Abstract from PubMed ==
In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III2IV2 supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O2 oxidoreductase activity without exogenous cytochrome c and includes a superoxide dismutase subunit that may detoxify reactive oxygen species produced during respiration. We found menaquinone bound in both the Qo and Qi sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c1 and soluble cytochrome c in canonical electron-transport chains, displays two conformations: one in which it provides a direct electronic link to complex IV and another in which it serves as an electrical switch interrupting the connection.

Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis.,Wiseman B, Nitharwal RG, Fedotovskaya O, Schafer J, Guo H, Kuang Q, Benlekbir S, Sjostrand D, Adelroth P, Rubinstein JL, Brzezinski P, Hogbom M Nat Struct Mol Biol. 2018 Dec;25(12):1128-1136. doi: 10.1038/s41594-018-0160-3., Epub 2018 Dec 5. PMID:30518849<ref>PMID:30518849</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6hwh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Adelroth P]]
[[Category: Benlekbir S]]
[[Category: Brzezinski P]]
[[Category: Fedotovskaya O]]
[[Category: Guo H]]
[[Category: Hogbom M]]
[[Category: Kuang Q]]
[[Category: Nitharwal RG]]
[[Category: Rubinstein JL]]
[[Category: Schafer J]]
[[Category: Sjostrand D]]
[[Category: Wiseman B]]