ArticlePloS one2011
Crystal structure of the pyrazinamidase of Mycobacterium tuberculosis: insights into natural and acquired resistance to pyrazinamide.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.
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Who cites it
62 citing papers in PubMed, 1 synthesis or guideline pooled it, 141 citations in OpenAlex.
- Systematic review of mutations in pyrazinamidase associated with pyrazinamide resistance in Mycobacterium tuberculosis clinical isolates.Antimicrobial agents and chemotherapy · 2015Pooled it
- The structural context of mutations in proteins predicts their effect on antibiotic resistance.eLife · 2026Article
- Predicting pyrazinamide resistance in Mycobacterium tuberculosis using a graph convolutional network.BMC microbiology · 2026Article
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Chemical genetic interactions elucidate pathways controlling tuberculosis antibiotic efficacy during infection.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genetic Analysis of Molecular Mechanisms of Drug Resistance inInfection and drug resistance · 2025Review
- Biphasic Medium Using Nicotinamide for Detection of Pyrazinamide Resistance inAntibiotics (Basel, Switzerland) · 2024Article
- Prediction of pyrazinamide resistance inJAC-antimicrobial resistance · 2024Article
- Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line.Genetics and molecular biology · 2023Article
- Structure activity relationship of pyrazinoic acid analogs as potential antimycobacterial agents.Bioorganic & medicinal chemistry · 2022Article
- A convolutional neural network highlights mutations relevant to antimicrobial resistance in Mycobacterium tuberculosis.Nature communications · 2022Article
- Article
- Structural and Dynamic Insights into the W68L, L85P, and T87A Mutations ofInternational journal of environmental research and public health · 2022Article
- Intracellular localisation of Mycobacterium tuberculosis affects efficacy of the antibiotic pyrazinamide.Nature communications · 2021Article
- A computational perspective on the dynamic behaviour of recurrent drug resistance mutations in the pncA gene fromRSC advances · 2021Article
- Computational modeling and bioinformatic analyses of functional mutations in drug target genes inComputational and structural biotechnology journal · 2021Article
- A Comprehensive Evaluation of GeneLEAD VIII DNA Platform Combined to Deeplex Myc-TBFrontiers in cellular and infection microbiology · 2021Article
- Structural and Genomic Insights Into Pyrazinamide Resistance inFrontiers in molecular biosciences · 2021Article
- Insights Into Mutations Induced Conformational Changes and Rearrangement of FeFrontiers in molecular biosciences · 2021Article
- Mechanistic analysis of A46V, H57Y, and D129N in pyrazinamidase associated with pyrazinamide resistance.Saudi journal of biological sciences · 2020Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pyrazinamidase (PncA) activates the first-line antituberculous drug pyrazinamide into pyrazinoic acid. The crystal structure of the Mycobacterium tuberculosis PncA protein has been determined, showing significant differences in the substrate binding cavity when compared to the pyrazinamidases from Pyrococcus horikoshii and Acinetobacter baumanii. In M. tuberculosis, this region was found to hold a Fe(2+) ion coordinated by one aspartate and three histidines, one of them corresponding to His57 which is replaced by Asp in Mycobacterium bovis, a species naturally resistant to pyrazinamide. The binding cavity also contains a Cys138-Asp8-Lys96 motif evocating a cysteine-based catalytic mechanism. Mutants have been constructed and investigated by kinetic and thermal shift assays, highlighting the importance of protein folding and thermal stability in the pyrazinamidase activity.
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