ArticleNature communications2021
Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- Recent advances in antituberculosis drugs and therapeutics: from mechanistic breakthroughs to clinical translation.Molecular biomedicine · 2026Review
- Redox-stratified macromolecule degradation supports microbial survival in the oligotrophic Kermadec Trench sediments.Nature communications · 2026Article
- Visualizing the mechanism of quinol oxidation and inhibition of aScience advances · 2026Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-resolved insights into hydrocarbon-transforming and nitrate-reducing microbial communities from deep petroleum reservoir cores of the Nashpa Oil Field, Pakistan.Frontiers in microbiology · 2026Article
- Mycobacterial respiratory chain enzymes and growth are inhibited by decylubiquinone.Communications biology · 2025Article
- Remission spectroscopy resolves the mechanism of action of bedaquiline within living mycobacteria.Nature communications · 2025Article
- Clear niche partitioning of nitrite-oxidizing bacteria from the bottom and the slope of Mariana Trench.Microbiome · 2025Article
- Carbon Monoxide and Prokaryotic Energy Metabolism.International journal of molecular sciences · 2025Review
- Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and aerobic respiration in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the Chemical Space of Mycobacterial Oxidative Phosphorylation Inhibitors Using Molecular Modeling.ChemMedChem · 2024Review
- CytochromeRSC medicinal chemistry · 2024Review
- Cryo-EM structures of a prokaryotic heme transporter CydDC.Protein & cell · 2023Article
- Structural basis of membrane machines that traffick and attach heme to cytochromes.The Journal of biological chemistry · 2023Article
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- Structure of mycobacterial respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Identification of 2-Aryl-Quinolone Inhibitors of CytochromeACS infectious diseases · 2023Article
- Response ofInternational journal of molecular sciences · 2022Article
- Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022Review
- Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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