Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF.
Bacterial Proteins
/ chemistry
Binding Sites
Catalysis
Cryoelectron Microscopy
Electron Transport
Models, Molecular
Multienzyme Complexes
/ chemistry
Mycobacterium smegmatis
/ chemistry
Oxidation-Reduction
Protein Subunits
/ chemistry
Structure-Activity Relationship
Succinate Dehydrogenase
/ chemistry
Succinic Acid
/ metabolism
Vitamin K 2
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
25 08 2020
25 08 2020
Historique:
received:
16
01
2020
accepted:
24
07
2020
entrez:
27
8
2020
pubmed:
28
8
2020
medline:
17
9
2020
Statut:
epublish
Résumé
Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria but little is known about the catalytic mechanisms they employ for succinate oxidation by menaquinone. Here, we present the 2.8 Å cryo-electron microscopy structure of a Mycobacterium smegmatis Sdh, which forms a trimer. We identified the membrane-anchored SdhF as a subunit of the complex. The 3 kDa SdhF forms a single transmembrane helix and this helix plays a role in blocking the canonically proximal quinone-binding site. We also identified two distal quinone-binding sites with bound quinones. One distal binding site is formed by neighboring subunits of the complex. Our structure further reveals the electron/proton transfer pathway for succinate oxidation by menaquinone. Moreover, this study provides further structural insights into the physiological significance of a trimeric respiratory complex II. The structure of the menaquinone binding site could provide a framework for the development of Sdh-selective anti-mycobacterial drugs.
Identifiants
pubmed: 32843629
doi: 10.1038/s41467-020-18011-9
pii: 10.1038/s41467-020-18011-9
pmc: PMC7447783
doi:
Substances chimiques
Bacterial Proteins
0
Multienzyme Complexes
0
Protein Subunits
0
Vitamin K 2
11032-49-8
Succinic Acid
AB6MNQ6J6L
Succinate Dehydrogenase
EC 1.3.99.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4245Commentaires et corrections
Type : ErratumIn
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