The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB

Schara 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

doi:10.1038/s41467-021-25537-z

Nature Communications (Sep 2021)

The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB

Schara 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

Affiliations

Schara Safarian: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics
Helen K. Opel-Reading: Department of Biochemistry, University of Otago
Di Wu: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics
Ahmad R. Mehdipour: Department of Theoretical Biophysics, Max Planck Institute of Biophysics
Kiel Hards: Department of Microbiology and Immunology, School of Biomedical Sciences, University of Otago
Liam K. Harold: Department of Microbiology and Immunology, School of Biomedical Sciences, University of Otago
Melanie Radloff: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics
Ian Stewart: Department of Chemistry, University of Otago
Sonja Welsch: Central Electron Microscopy Facility, Max Planck Institute of Biophysics
Gerhard Hummer: Department of Theoretical Biophysics, Max Planck Institute of Biophysics
Gregory M. Cook: Department of Microbiology and Immunology, School of Biomedical Sciences, University of Otago
Kurt L. Krause: Department of Biochemistry, University of Otago
Hartmut Michel: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics

DOI: https://doi.org/10.1038/s41467-021-25537-z
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 10

Abstract

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M. tuberculosis cytochrome bd oxidase is of interest as a TB drug target. Here, the authors present the 2.5 Å cryo-EM structure of M. tuberculosis cytochrome bd oxidase and identify a disulfide bond within the canonical quinol binding and oxidation domain (Q-loop) and a menaquinone-9 binding site at heme b 595.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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