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1v9e

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[[Image:1v9e.gif|left|200px]]
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{{STRUCTURE_1v9e| PDB=1v9e | SCENE= }}
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'''Crystal Structure Analysis of Bovine Carbonic Anhydrase II'''
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===Crystal Structure Analysis of Bovine Carbonic Anhydrase II===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15039588}}
==About this Structure==
==About this Structure==
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[[Category: Twisted beta sheet]]
[[Category: Twisted beta sheet]]
[[Category: Zinc metalloenzyme]]
[[Category: Zinc metalloenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:23:18 2008''

Revision as of 07:23, 29 July 2008

Template:STRUCTURE 1v9e

Crystal Structure Analysis of Bovine Carbonic Anhydrase II

Template:ABSTRACT PUBMED 15039588

About this Structure

1V9E is a Single protein structure of sequence from Bos taurus. 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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