Ariyoshi M, Vassylyev D G, Iwasaki H, Nakamura H, Shinagawa H, Morikawa K
Protein Engineering Research Institute, Osaka, Japan.
Cell. 1994 Sep 23;78(6):1063-72. doi: 10.1016/0092-8674(94)90280-1.
The crystal structure of the RuvC protein, a Holliday junction resolvase from E. coli, has been determined at 2.5 A resolution. The enzyme forms a dimer of 19 kDa subunits related by a dyad axis. Together with results from extensive mutational analyses, the refined structure reveals that the catalytic center, comprising four acidic residues, lies at the bottom of a cleft that nicely fits a DNA duplex. The structural features of the dimer, with a 30 A spacing between the two catalytic centers, provide a substantially defined image of the Holliday junction architecture. The folding topology in the vicinity of the catalytic site exhibits a striking similarity to that of RNAase H1 from E. coli.
已确定来自大肠杆菌的霍利迪连接体解离酶RuvC蛋白的晶体结构，分辨率为2.5埃。该酶形成由二元轴相关的19 kDa亚基二聚体。结合广泛的突变分析结果，优化后的结构表明，由四个酸性残基组成的催化中心位于一个恰好能容纳DNA双链的裂隙底部。二聚体的结构特征是两个催化中心之间间隔30埃，这为霍利迪连接体结构提供了一个基本明确的图像。催化位点附近的折叠拓扑结构与大肠杆菌核糖核酸酶H1的折叠拓扑结构惊人地相似。
