Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III.
Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III.
复制标题
DOI：
--
复制
发表时间：
2001
期刊：
影响因子：
64.5
通讯作者：
D. Jeruzalmi;M. O’Donnell;J. Kuriyan
中科院分区：
文献类型：
--
作者：
D. Jeruzalmi;M. O’Donnell;J. Kuriyan
伽马复合体是一种AAA+ATPase，是真核细胞复制因子C(RFC)的细菌同源物，它将滑动钳(β，与增殖细胞核抗原同源)加载到DNA上。2.7A/3.0A的晶体结构揭示了亚基的五聚体排列，化学计量比为‘：伽马(3)：三角洲。亚基的C-末端结构域形成圆形环，支持伽马电机的N-末端ATP结合域以及Delta定子和Delta扳手的结构相关结构域的不对称排列。这种结构表明了一种机制，通过这种机制，伽马络合物在关闭状态和开放形式之间切换，在关闭状态下，Delta的β相互作用元素被Delta‘隐藏，而在开放状态下，Delta可以自由结合到β。
The gamma complex, an AAA+ ATPase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp (beta, homologous to PCNA) onto DNA. The 2.7/3.0 A crystal structure of gamma complex reveals a pentameric arrangement of subunits, with stoichiometry delta':gamma(3):delta. The C-terminal domains of the subunits form a circular collar that supports an asymmetric arrangement of the N-terminal ATP binding domains of the gamma motor and the structurally related domains of the delta' stator and the delta wrench. The structure suggests a mechanism by which the gamma complex switches between a closed state, in which the beta-interacting element of delta is hidden by delta', and an open form similar to the crystal structure, in which delta is free to bind to beta.