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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of bovine carbonic anhydrase II at 1.95 A resolution.
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Structure of bovine carbonic anhydrase II at 1.95 A resolution.

机译：牛碳酸酐酶II 1.95的结构一项决议。

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摘要

Carbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the reversible hydration of CO(2) to HCO(3)(-). In eukaryotes, the enzyme plays a role in various physiological functions, including interconversion between CO(2) and HCO(3)(-) in intermediary metabolism, facilitated diffusion of CO(2), 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.
机译：碳酸酐酶(CA)是一个zinc-containing酶催化的可逆水合作用有限公司(2)HCO(3)(-)。在各种生理功能中发挥作用,包括(2)和之间的互变现象HCO(3)(-)在中间代谢,促进有限公司(2)扩散、pH稳态和离子交通工具。脱水酶II (BCA II)已经决定了1.95分子置换和精制通过模拟退火和个人解决b因子细化。BCA II结构为19.4%。c端结结构相似观察到在人类CA II。在活动现场协调三个组氨酸和一个假定的水分子四面体几何。揭示了一个可能的替代proton-wire途径不同于HCA II。

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