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Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.
Structural highlights
FunctionPublication Abstract from PubMedCarbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate and proton. Currently, CA inhibitors are widely used as antiglaucoma, anticancer, and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi, and bacteria has emerged as a new research line. In this article, the X-ray crystal structure of beta-CA from Burkholderia pseudomallei was reported. The X-ray crystal structure of this new enzyme was solved at 2.7 A resolution, revealing a tetrameric type II beta-CA with a "closed" active site in which the zinc is tetrahedrally coordinated to Cys46, Asp48, His102, and Cys105. B. pseudomallei is known to encode at least two CAs, a beta-CA, and a gamma-CA. These proteins, playing a pivotal role in its life cycle and pathogenicity, offer a novel therapeutic opportunity to obtain antibiotics with a different mechanism of action. Furthermore, the new structure can provide a clear view of the beta-CA mechanism of action and the possibility to find selective inhibitors for this class of CAs. Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei.,Angeli A, Ferraroni M, Pinteala M, Maier SS, Simionescu BC, Carta F, Del Prete S, Capasso C, Supuran CT Molecules. 2020 May 12;25(10). pii: molecules25102269. doi:, 10.3390/molecules25102269. PMID:32408533[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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