1V9E

Crystal Structure Analysis of Bovine Carbonic Anhydrase II

Summary for 1V9E

• Entry DOI: 10.2210/pdb1v9e/pdb
• Related: 1V9I
• Descriptor: Carbonic anhydrase II, ZINC ION (3 entities in total)
• Functional Keywords: high-resolution, twisted beta sheet, zinc metalloenzyme, lyase
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P00921
• Total number of polymer chains: 2
• Total formula weight: 58171.94

Authors

Saito, R.,Sato, T.,Ikai, A.,Tanaka, N. (deposition date: 2004-01-26, release date: 2004-02-10, Last modification date: 2023-12-27)

Primary citation

Saito, R.,Sato, T.,Ikai, A.,Tanaka, N.
Structure of bovine carbonic anhydrase II at 1.95 A resolution.
Acta Crystallogr.,Sect.D, 60:792-795, 2004

PubMed Abstract: 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.

PubMed: 15039588
DOI: 10.1107/S0907444904003166

Experimental method

X-RAY DIFFRACTION (1.95 Å)