ArticleStructure (London, England : 1993)2021
Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 24 citations in OpenAlex.
- Single-atom substitution redirects KatG reactivity from cofactor biogenesis to stereoselective sulfoxidation.Nature communications · 2026Article
- Uncovering the structural impact of KatG Ser315 mutations in Mycobacterium tuberculosis via cryo-EM.Protein science : a publication of the Protein Society · 2026Article
- Future Research Directions on Mycobacterium tuberculosis Proteins.Advances in experimental medicine and biology · 2026Review
- Phase-Specific Antibiotic Resistance Mechanisms in anbioRxiv : the preprint server for biology · 2025Article
- Computational analyses of drug resistance mutations in katG and emb complexes in Mycobacterium tuberculosis.Proteins · 2025Article
- Characterization of a catalase-peroxidase variant (L333V-KatG) identified in an INH-resistantBiochemistry and biophysics reports · 2024Article
- Quantitative measurement of antibiotic resistance in Mycobacterium tuberculosis reveals genetic determinants of resistance and susceptibility in a target gene approach.Nature communications · 2024Article
- Identification of 2-(Frontiers in chemistry · 2024Article
- Quantitative measurement of antibiotic resistance inResearch square · 2023Article
- Aromatic hydrazides: A potential solution for Acinetobacter baumannii infections.European journal of medicinal chemistry · 2023Article
- Large-scale genomic analysis of Mycobacterium tuberculosis reveals extent of target and compensatory mutations linked to multi-drug resistant tuberculosis.Scientific reports · 2023Article
- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- Deciphering Isoniazid Drug Resistance Mechanisms on DimericACS omega · 2022Article
- CryoEM analysis of small plant biocatalysts at sub-2 Å resolution.Acta crystallographica. Section D, Structural biology · 2022Article
- Recent Insights into the Structure and Function of Mycobacterial Membrane Proteins Facilitated by Cryo-EM.The Journal of membrane biology · 2021Review
- Structure-Guided Computational Approaches to Unravel Druggable Proteomic Landscape ofFrontiers in molecular biosciences · 2021Review
- Computational modeling and bioinformatic analyses of functional mutations in drug target genes inComputational and structural biotechnology journal · 2021Article
- Novel dynamic residue network analysis approaches to study allosteric modulation: SARS-CoV-2 MComputational and structural biotechnology journal · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Resolution advances in cryoelectron microscopy (cryo-EM) now offer the possibility to visualize structural effects of naturally occurring resistance mutations in proteins and also of understanding the binding mechanisms of small drug molecules. In Mycobacterium tuberculosis the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. We present a cryo-EM methodology for structural and functional characterization of KatG and INH resistance variants. The cryo-EM structure of the 161 kDa KatG dimer in the presence of INH is reported to 2.7 Å resolution allowing the observation of potential INH binding sites. In addition, cryo-EM structures of two INH resistance variants, identified from clinical isolates, W107R and T275P, are reported. In combination with electronic absorbance spectroscopy our cryo-EM approach reveals how these resistance variants cause disorder in the heme environment preventing heme uptake and retention, providing insight into INH resistance.
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