ArticlePloS one2011
Crystal structure of a novel esterase Rv0045c from Mycobacterium tuberculosis.
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 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.Protein science : a publication of the Protein Society · 2021Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- Microbial esterases and ester prodrugs: An unlikely marriage for combating antibiotic resistance.Drug development research · 2019Review
- A proposed update for the classification and description of bacterial lipolytic enzymes.PeerJ · 2019Article
- Fluorogenic structure activity library pinpoints molecular variations in substrate specificity of structurally homologous esterases.The Journal of biological chemistry · 2018Article
- Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Biochemistry · 2016Article
- Conserved tyrosine 182 residue in hyperthermophilic esterase EstE1 plays a critical role in stabilizing the active site.Extremophiles : life under extreme conditions · 2016Article
- Mechanistic insights from molecular dynamic simulation of Rv0045c esterase in Mycobacterium tuberculosis.Journal of molecular modeling · 2015Article
- Characterization of an acid inducible lipase Rv3203 from Mycobacterium tuberculosis H37Rv.Molecular biology reports · 2014Article
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Authors and funding
10 authors.
Funding
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Abstract
There are at least 250 enzymes in Mycobacterium tuberculosis (M. tuberculosis) involved in lipid metabolism. Some of the enzymes are required for bacterial survival and full virulence. The esterase Rv0045c shares little amino acid sequence similarity with other members of the esterase/lipase family. Here, we report the 3D structure of Rv0045c. Our studies demonstrated that Rv0045c is a novel member of α/β hydrolase fold family. The structure of esterase Rv0045c contains two distinct domains: the α/β fold domain and the cap domain. The active site of esterase Rv0045c is highly conserved and comprised of two residues: Ser154 and His309. We proposed that Rv0045c probably employs two kinds of enzymatic mechanisms when hydrolyzing C-O ester bonds within substrates. The structure provides insight into the hydrolysis mechanism of the C-O ester bond, and will be helpful in understanding the ester/lipid metabolism in M. tuberculosis.
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