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Crystal structure of a gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomalleiCrystal structure of a gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei
Structural highlights
FunctionPublication Abstract from PubMedMelioidosis is a severe disease caused by the highly pathogenic gram-negative bacterium Burkholderia pseudomallei. Several studies have highlighted the broad resistance of this pathogen to many antibiotics and pointed out the pivotal importance of improving the pharmacological arsenal against it. Since gamma-carbonic anhydrases (gamma-CAs) have been recently introduced as potential and novel antibacterial drug targets, in this paper, we report a detailed characterization of BpsgammaCA, a gamma-CA from B. pseudomallei by a multidisciplinary approach. In particular, the enzyme was recombinantly produced and biochemically characterized. Its catalytic activity at different pH values was measured, the crystal structure was determined and theoretical pKa calculations were carried out. Results provided a snapshot of the enzyme active site and dissected the role of residues involved in the catalytic mechanism and ligand recognition. These findings are an important starting point for developing new anti-melioidosis drugs targeting BpsgammaCA. Biochemical, structural, and computational studies of a gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.,Di Fiore A, De Luca V, Langella E, Nocentini A, Buonanno M, Maria Monti S, Supuran CT, Capasso C, De Simone G Comput Struct Biotechnol J. 2022 Jul 27;20:4185-4194. doi:, 10.1016/j.csbj.2022.07.033. eCollection 2022. PMID:36016712[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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