1v9e
Crystal Structure Analysis of Bovine Carbonic Anhydrase IICrystal Structure Analysis of Bovine Carbonic Anhydrase II
Structural highlights
FunctionCAH2_BOVIN Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCarbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the reversible hydration of CO2 to HCO3-. In eukaryotes, the enzyme plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport. The structure of bovine carbonic anhydrase II (BCA II) has been determined by molecular replacement and refined to 1.95 A resolution by simulated-annealing and individual B-factor refinement. The final R factor for the BCA II structure was 19.4%. BCA II has a C-terminal knot structure similar to that observed in human CA II. It contains one zinc ion in the active site coordinated to three histidines and one putative water molecule in a tetrahedral geometry. The structure of BCA II reveals a probable alternative proton-wire pathway that differs from that of HCA II. Structure of bovine carbonic anhydrase II at 1.95 A resolution.,Saito R, Sato T, Ikai A, Tanaka N Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):792-5. Epub 2004, Mar 23. PMID:15039588[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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