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

Medicine and Health

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

S. Safarian, H. K. Opel-reading, et al.

Explore groundbreaking research from Schara Safarian and colleagues that unveils the cryo-EM structure of cytochrome bd oxidase from Mycobacterium tuberculosis. This study reveals a novel MK-9-binding site and a unique disulfide bond, paving the way for the development of targeted drugs to combat tuberculosis and reduce drug resistance.

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Playback language: English
Abstract
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. This paper presents the cryo-EM structure of the cytochrome *bd* oxidase from *M. tuberculosis* at 2.5 Å, revealing a previously unknown MK-9-binding site and a unique disulfide bond. These insights will form the basis for designing highly specific drugs targeting this enzyme.
Publisher
Nature Communications
Published On
Sep 02, 2021
Authors
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
Tags
tuberculosis
drug resistance
cytochrome bd oxidase
MK-9-binding site
cryogenic electron microscopy
Mycobacterium tuberculosis
enzyme complexes

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