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TitleStructure of a functional obligate complex IIIIV respiratory supercomplex from Mycobacterium smegmatis.
Journal, issue, pagesNat Struct Mol Biol, Vol. 25, Issue 12, Page 1128-1136, Year 2018
Publish dateDec 5, 2018
AuthorsBenjamin Wiseman / Ram Gopal Nitharwal / Olga Fedotovskaya / Jacob Schäfer / Hui Guo / Qie Kuang / Samir Benlekbir / Dan Sjöstrand / Pia Ädelroth / John L Rubinstein / Peter Brzezinski / Martin Högbom /
PubMed AbstractIn 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 ...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 IIIIV supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O 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 Q and Q sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c 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.
External linksNat Struct Mol Biol / PubMed:30518849
MethodsEM (single particle)
Resolution3.3 Å
Structure data

0289

6hwh

EMDB-0289, PDB-6hwh:
Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-MQ9:
MENAQUINONE-9

ChemComp-CU:
COPPER (II) ION

ChemComp-HAS:
HEME-AS

ChemComp-HEC:
HEME C

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

Source
  • Mycobacterium smegmatis str. MC2 155 (bacteria)
  • mycobacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
  • mycobacterium smegmatis mc2 155 (bacteria)
KeywordsELECTRON TRANSPORT / Membrane Protein / Cryo-EM / Respiratory supercomplex / Mycobacterium

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