Structural highlights
Function[A0A1G5JF57_ACIBA] Reversible hydration of carbon dioxide.[RuleBase:RU003956] Publication Abstract from PubMedPseudomonas aeruginosa (P. aeruginosa) is a gram-negative facultative anaerobe belonging to the Pseudomonadaceae family. It is a multi-drug resistant opportunistic human pathogen and a common cause of life-threatening nosocomial infections, and is a key bacterial agent in cystic fibrosis and endocarditis diseases. The bacterium exhibits intrinsic resistance to most antibacterial agents, including aminoglycosides and quinolones. Hence, the identification of new drug targets for P. aeruginosa are ongoing. PsCA3 is a beta-class carbonic anhydrase (beta-CA) catalyzing the reversible hydration of carbon dioxide to bicarbonate and represents a new class of antimicrobial target. Previously, inhibitor-screening studies of psCA3 have shown a series of small anions including sulfamide (SFN), imidazole (IMD), and 4-methyl imidazole (4MI) and thiocyanate (SCN) inhibit the enzyme with efficiencies in the micro- to millimolar range. Here, the X-ray crystal structures of these inhibitors in complex with psCA3 are presented and compared to human CA II. This structural survey into the binding modes of small anions forms the foundation for the development of inhibitors against beta-CAs and more selective inhibitors against P. aeruginosa. Structural Mapping of Anion inhibitors to beta-Carbonic Anhydrase psCA3 from Pseudomonas aeruginosa.,Murray A, Aggarwal M, Pinard M, Vullo D, Patrauchan M, Supuran CT, McKenna R ChemMedChem. 2018 Aug 7. doi: 10.1002/cmdc.201800375. PMID:30088334[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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