The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile.
The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile.
复制标题
枯草杆菌蛋白酶嘉士伯在无水二恶烷中的晶体结构及其与水和乙腈中晶体结构的比较。
DOI：
10.1073/pnas.94.9.4250
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发表时间：
1997
影响因子：
11.1
通讯作者：
Klibanov,AM
中科院分区：
文献类型：
--
作者：
Schmitke,JL;Stern,LJ;Klibanov,AM
丝氨酸蛋白酶枯草菌素嘉士伯在无水二氧六环中的x射线晶体结构已测定到2.6-Å分辨率。发现酶的结构与以前在水和乙腈中确定的结构几乎没有区别。二氧六环和水结构之间侧链构象的微小变化与在不同水体系中观察到的两种结构之间的变化幅度相同。已经检测到七个酶结合的二氧六环分子，每个分子都可能与枯草菌素氢键供体或结合水形成至少一个氢键。两个结合的二氧六环分子位于活性位点区域，一个位于P2，另一个连接P1 ‘和P3 ’口袋。另外五个二氧六环分子位于枯草菌素表面的蛋白间晶体接触处。二氧六环结构中结合溶剂的位置与乙腈和水结构中的结合溶剂的位置不同。
The x-ray crystal structure of the serine protease subtilisin Carlsberg in anhydrous dioxane has been determined to 2.6-Å resolution. The enzyme structure is found to be nearly indistinguishable from the structures previously determined in water and acetonitrile. Small changes in the side-chain conformations between the dioxane and water structures are of the same magnitude as those observed between two structures in different aqueous systems. Seven enzyme-bound dioxane molecules have been detected, each potentially forming at least one hydrogen bond with a subtilisin hydrogen-bond donor or bound water. Two of the bound dioxane molecules are in the active-site region, one in the P2 and another bridging the P1′ and P3′ pockets. The other five dioxane molecules are located on the surface of subtilisin at interprotein crystal contacts. The locations of the bound solvent in the dioxane structure are distinct from those in the structures in acetonitrile and in water.