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TitleThe cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 5236, Year 2021
Publish dateSep 2, 2021
AuthorsSchara Safarian / Helen K Opel-Reading / Di Wu / Ahmad R Mehdipour / Kiel Hards / Liam K Harold / Melanie Radloff / Ian Stewart / Sonja Welsch / Gerhard Hummer / Gregory M Cook / Kurt L Krause / Hartmut Michel /
PubMed AbstractNew drugs are urgently needed to combat the global TB epidemic. Targeting simultaneously multiple respiratory enzyme complexes of Mycobacterium tuberculosis is regarded as one of the most effective ...New drugs are urgently needed to combat the global TB epidemic. Targeting simultaneously multiple respiratory enzyme complexes of Mycobacterium tuberculosis is regarded as one of the most effective treatment options to shorten drug administration regimes, and reduce the opportunity for the emergence of drug resistance. During infection and proliferation, the cytochrome bd oxidase plays a crucial role for mycobacterial pathophysiology by maintaining aerobic respiration at limited oxygen concentrations. Here, we present the cryo-EM structure of the cytochrome bd oxidase from M. tuberculosis at 2.5 Å. In conjunction with atomistic molecular dynamics (MD) simulation studies we discovered a previously unknown MK-9-binding site, as well as a unique disulfide bond within the Q-loop domain that defines an inactive conformation of the canonical quinol oxidation site in Actinobacteria. Our detailed insights into the long-sought atomic framework of the cytochrome bd oxidase from M. tuberculosis will form the basis for the design of highly specific drugs to act on this enzyme.
External linksNat Commun / PubMed:34475399 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.3 Å
Structure data

12451

7nkz

EMDB-12451, PDB-7nkz:
Cryo-EM structure of the cytochrome bd oxidase from M. tuberculosis at 2.5 A resolution
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-12532:
Cryo-EM structure of the cytochrome bd oxidase from M. tuberculosis in presence of AD3-11 at 2.8 A resolution
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-12533:
Cryo-EM structure of the cytochrome bd oxidase from M. tuberculosis in presence of Aurachin D at 3.3 A resolution
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-OXY:
OXYGEN MOLECULE / Oxygen

ChemComp-MQ9:
MENAQUINONE-9 / Vitamin K2

ChemComp-HDD:
CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE / Heme

ChemComp-HEB:
HEME B/C

ChemComp-HOH:
WATER / Water

Source
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsMEMBRANE PROTEIN / Terminal oxidase Oxidoreductase Oxygen reductase bd oxidase

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