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Crystal structure of the b-carbonic anhydrase CafA of the fungal pathogen Aspergillus fumigatusCrystal structure of the b-carbonic anhydrase CafA of the fungal pathogen Aspergillus fumigatus
Structural highlights
FunctionQ4WQ18_ASPFU Reversible hydration of carbon dioxide.[RuleBase:RU003956] Publication Abstract from PubMedThe beta-class of carbonic anhydrases (beta-CAs) are zinc metalloenzymes widely distributed in the fungal kingdom that play essential roles in growth, survival, differentiation, and virulence by catalyzing the reversible interconversion of carbon dioxide (CO2) and bicarbonate (HCO3(-)). Herein, we report the biochemical and crystallographic characterization of the beta-CA CafA from the fungal pathogen Aspergillus fumigatus, the main causative agent of invasive aspergillosis. CafA exhibited apparent in vitro CO2 hydration activity in neutral to weak alkaline conditions, but little activity at acidic pH. The high-resolution crystal structure of CafA revealed a tetramer comprising a dimer of dimers, in which the catalytic zinc ion is tetrahedrally coordinated by three conserved residues (C119, H175, C178) and an acetate anion presumably acquired from the crystallization solution, indicating a freely accessible open conformation. Furthermore, knowledge of the structure of CafA in complex with the potent inhibitor acetazolamide, together with its functional intolerance of nitrate (NO3(-)) ions, could be exploited to develop new antifungal agents for the treatment of invasive aspergillosis. Crystal Structure of beta-Carbonic Anhydrase CafA from the Fungal Pathogen Aspergillus fumigatus.,Kim S, Yeon J, Sung J, Jin MS Mol Cells. 2020 Sep 30;43(9):831-840. doi: 10.14348/molcells.2020.0168. PMID:32975213[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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