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TitleArchitecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 15, Year 2021
Publish dateApr 13, 2021
AuthorsXiaoting Zhou / Yan Gao / Weiwei Wang / Xiaolin Yang / Xiuna Yang / Fengjiang Liu / Yanting Tang / Sin Man Lam / Guanghou Shui / Lu Yu / Changlin Tian / Luke W Guddat / Quan Wang / Zihe Rao / Hongri Gong /
PubMed AbstractComplex II, also known as succinate dehydrogenase (SQR) or fumarate reductase (QFR), is an enzyme involved in both the Krebs cycle and oxidative phosphorylation. Mycobacterial Sdh1 has recently been ...Complex II, also known as succinate dehydrogenase (SQR) or fumarate reductase (QFR), is an enzyme involved in both the Krebs cycle and oxidative phosphorylation. Mycobacterial Sdh1 has recently been identified as a new class of respiratory complex II (type F) but with an unknown electron transfer mechanism. Here, using cryoelectron microscopy, we have determined the structure of Sdh1 in the presence and absence of the substrate, ubiquinone-1, at 2.53-Å and 2.88-Å resolution, respectively. Sdh1 comprises three subunits, two that are water soluble, SdhA and SdhB, and one that is membrane spanning, SdhC. Within these subunits we identified a quinone-binding site and a rarely observed Rieske-type [2Fe-2S] cluster, the latter being embedded in the transmembrane region. A mutant, where two His ligands of the Rieske-type [2Fe-2S] were changed to alanine, abolished the quinone reduction activity of the Sdh1. Our structures allow the proposal of an electron transfer pathway that connects the substrate-binding and quinone-binding sites. Given the unique features of Sdh1 and its essential role in , these structures will facilitate antituberculosis drug discovery efforts that specifically target this complex.
External linksProc Natl Acad Sci U S A / PubMed:33876763 / PubMed Central
MethodsEM (single particle)
Resolution2.53 - 2.88 Å
Structure data

30594

7d6v

EMDB-30594, PDB-7d6v:
Mycobacterium smegmatis Sdh1 in complex with UQ1
Method: EM (single particle) / Resolution: 2.53 Å

30595

7d6x

EMDB-30595, PDB-7d6x:
Mycobacterium smegmatis Sdh1 complex in the apo form
Method: EM (single particle) / Resolution: 2.88 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-F3S:
FE3-S4 CLUSTER

ChemComp-UQ1:
UBIQUINONE-1

ChemComp-PEV:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / POPE, phospholipid*YM

Source
  • Mycolicibacterium smegmatis MC2 51 (bacteria)
  • mycolicibacterium smegmatis (bacteria)
KeywordsOXIDOREDUCTASE / succinate dehydrogenase / electron transport chain / Mycobacterium smegmatis / Sdh1 / SQR

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