7ZW9

Crystal structure of a gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei

Summary for 7ZW9

• Entry DOI: 10.2210/pdb7zw9/pdb
• Descriptor: Bacterial transferase hexapeptide family protein, ZINC ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: bacterial target, lyase
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 1
• Total formula weight: 22621.09

Authors

Di Fiore, A.,De Simone, G. (deposition date: 2022-05-19, release date: 2022-09-07, Last modification date: 2024-01-31)

Primary citation

Di Fiore, A.,De Luca, V.,Langella, E.,Nocentini, A.,Buonanno, M.,Maria Monti, S.,Supuran, C.T.,Capasso, C.,De Simone, G.
Biochemical, structural, and computational studies of a gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.
Comput Struct Biotechnol J, 20:4185-4194, 2022

PubMed Abstract: Melioidosis is a severe disease caused by the highly pathogenic gram-negative bacterium . 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 γ-carbonic anhydrases (γ-CAs) have been recently introduced as potential and novel antibacterial drug targets, in this paper, we report a detailed characterization of BpsγCA, a γ-CA from . 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 BpsγCA.

PubMed: 36016712
DOI: 10.1016/j.csbj.2022.07.033

Experimental method

X-RAY DIFFRACTION (2.1 Å)