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TitleCryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4621, Year 2021
Publish dateJul 30, 2021
AuthorsWeiwei Wang / Yan Gao / Yanting Tang / Xiaoting Zhou / Yuezheng Lai / Shan Zhou / Yuying Zhang / Xiuna Yang / Fengjiang Liu / Luke W Guddat / Quan Wang / Zihe Rao / Hongri Gong /
PubMed AbstractCytochromes bd are ubiquitous amongst prokaryotes including many human-pathogenic bacteria. Such complexes are targets for the development of antimicrobial drugs. However, an understanding of the ...Cytochromes bd are ubiquitous amongst prokaryotes including many human-pathogenic bacteria. Such complexes are targets for the development of antimicrobial drugs. However, an understanding of the relationship between the structure and functional mechanisms of these oxidases is incomplete. Here, we have determined the 2.8 Å structure of Mycobacterium smegmatis cytochrome bd by single-particle cryo-electron microscopy. This bd oxidase consists of two subunits CydA and CydB, that adopt a pseudo two-fold symmetrical arrangement. The structural topology of its Q-loop domain, whose function is to bind the substrate, quinol, is significantly different compared to the C-terminal region reported for cytochromes bd from Geobacillus thermodenitrificans (G. th) and Escherichia coli (E. coli). In addition, we have identified two potential oxygen access channels in the structure and shown that similar tunnels also exist in G. th and E. coli cytochromes bd. This study provides insights to develop a framework for the rational design of antituberculosis compounds that block the oxygen access channels of this oxidase.
External linksNat Commun / PubMed:34330928 / PubMed Central
MethodsEM (single particle)
Resolution2.79 - 2.87 Å
Structure data

30582

7d5i

EMDB-30582, PDB-7d5i:
Structure of Mycobacterium smegmatis bd complex in the apo-form.
Method: EM (single particle) / Resolution: 2.79 Å

EMDB-31302:
Cryo-EM map of Mycobacterium smegmatis bd complex pre-incubated with aurachin D(AD)
Method: EM (single particle) / Resolution: 2.87 Å

Chemicals

ChemComp-HEB:
HEME B/C

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

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
  • Mycolicibacterium smegmatis MC2 51 (bacteria)
KeywordsOXIDOREDUCTASE / Mycobacterium smegmatis / electron transfer chain

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