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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer.
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The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer.

机译：碳酸酐酶的精致的原子结构二世在1.05一项决议:化学的影响救援的质子转移。

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摘要

Using synchrotron radiation and a CCD detector, X-ray data have been collected at 100 K for the His64Ala mutant of human carbonic anhydrase II complexed with 4-methylimidazole (4-MI) to a maximal 1.05 A resolution, allowing full anisotropic least-squares refinement. The refined model has a conventional R factor of 15.7% for all reflections. The C(alpha) coordinates of the model presented here have an r.m.s. deviation of 0.10 A relative to the previously determined structure at 1.6 A resolution. Several amino-acid residues (six of the 255 observed) have been identified with multiple rotamer side-chain conformations. C, N and O atoms can be differentiated with selective electron-density map contouring. The estimated standard deviations for all main-chain non-H atom bond lengths and angles are 0.013 and 0.030 A, respectively, based on unrestrained full-matrix least-squares refinement. This structure gives detailed information about the tetrahedrally arranged zinc ion coordinated by three histidine N atoms(His94 N(epsilon 2), His96 N(epsilon2) and His119 N(delta1)) and a water/hydroxide, the multiple binding sites of the proton chemical rescue molecule 4-MI and the solvent networks linking the zinc-bound water/hydroxide and 4-MI molecules. This structure presents the highest resolution structure of a carbonic anhydrase isozyme so far determined and adds to the understanding of proton-transfer processes.
机译：利用同步辐射和CCD探测器,x射线数据已经收集了在100 KHis64Ala人类碳酸酐酶II的突变包裹着4-methylimidazole (4-MI)最大1.05一项决议,允许充分各向异性最小二乘优化。模型有一个传统的R因子为15.7%所有的反射。本文介绍的模型有一个r.m.s.偏差的相对于0.10之前确定1.6结构解析。残留物(6 255年观察到的)与多个旋转异构体侧链构象。分化与选择性的电子密度地图轮廓。为所有主链原子non-H债券长度和角是0.013和0.030,分别在无节制的全矩阵最小二乘细化。四面体地安排锌的相关信息由三个组氨酸N原子(His94离子协调N(ε2),His96 N (epsilon2)和His119N (delta1))和水/氢氧根,多个结合位点的质子化学救援分子4-MI和溶剂网络链接zinc-bound水/氢氧根和4-MI分子。解决碳酸酐酶的结构同工酶到目前为止确定和增加了对质子转移过程的理解。

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