REFINEMENT OF THE STRUCTURE OF BOVINE SEMINAL RIBONUCLEASE
REFINEMENT OF THE STRUCTURE OF BOVINE SEMINAL RIBONUCLEASE
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DOI：
10.1002/bip.360220142
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发表时间：
1983-01-01
期刊：
影响因子：
2.9
通讯作者：
ZAGARI, A
中科院分区：
文献类型：
--
作者：
CAPASSO, S;GIORDANO, F;ZAGARI, A
我们在这里报告细化在2.5‐Å分辨率的牛精液核糖核酸酶，二聚体共价酶的x射线晶体结构。这种蛋白质在不对称单元中与一个分子结晶，由两个具有相同化学序列的亚基组成，它们通过一条几乎精确的二轴相连。亚基的三级结构与胰酶相似，表现出相似的催化性能。在互反空间和实空间中使用约束最小二乘法进行了细化。对二聚体中亚基的组合进行了描述和讨论。
We report here the refinement at 2.5‐Å resolution of the x‐ray crystal structure of bovine seminal ribonuclease, a dimeric covalent enzyme. The protein, which crystallizes with one molecule in the asymmetric unit, consists of two subunits of identical chemical sequences, related by an almost exact binary axis. The tertiary structure of the subunits is similar to that of the pancreatic enzyme, which shows similar catalytic properties. The refinement was carried out using the restrained least‐squares procedure both in the reciprocal and real spaces. The assemblage of the subunits in the dimer is described and discussed.