STRUCTURAL ANALYSIS OF RUVC RESOLVASE & ITS DNA SUBSTRATE

RUVC 解析酶的结构分析

• 批准号: 6586657
• 负责人: CHRISTIN A FREDERICK
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586657
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; genome; proteins; radiography; structural biology

RuvC is the only known endonuclease to resolve the four-way DNA complex better known as the Holliday junction. X-ray crystallographic studies reveal the active site of RuvC is topologically similar to the catalytic domain of other polynucleotidyl transferases such as HIV-1 Integrase, RNAse H and MuA. We report the successful crystallization of four sequence specific RuvC-Holliday junction complexes and their Bromine and Iodine derivatives. These crystal complexes diffract to 2.8 E resolution with conventional sources. Synchrotron radiation will greatly facilitate the determination of these structures in two ways: high resolution reflections will show greater intensity over sigma values, and the highly collimated beam will decrease the amount of diffuse scattering.

RuvC 是唯一已知的可解析四向 DNA 的核酸内切酶 复合体更广为人知的是霍利迪路口。 X射线晶体学 研究表明 RuvC 的活性位点在拓扑上与 其他多核苷酸转移酶（例如 HIV-1）的催化结构域 整合酶、RNAse H 和 MuA。 我们报告结晶成功 四个序列特异性 RuvC-Holliday 连接复合物及其 溴和碘衍生物。 这些晶体复合物衍射 传统光源的 2.8 E 分辨率。 同步辐射 将极大地方便在两个方面确定这些结构 方式：高分辨率反射将显示出更大的强度 西格玛值，高度准直的光束会减少量 的漫散射。