1v9e
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(New page: 200px<br /><applet load="1v9e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v9e, resolution 1.95Å" /> '''Crystal Structure An...)
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Revision as of 02:24, 21 November 2007
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Crystal Structure Analysis of Bovine Carbonic Anhydrase II
Overview
Carbonic 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.
About this Structure
1V9E is a Single protein structure of sequence from Bos taurus with ZN as ligand. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
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
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