Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimer

被引：6

作者：

Tondnevis, Farzaneh ^{[1
]}

Gillilan, Richard E. ^{[2
]}

Bloom, Linda B. ^{[1
]}

McKenna, Robert ^{[1
]}

机构：

[1] Univ Florida, Biochem & Mol Biol, Gainesville, FL 32610 USA

[2] Cornell Univ, Cornell High Energy Synchrotron Source, Ithaca, NY 14853 USA

来源：

STRUCTURAL DYNAMICS-US | 2015年 / 2卷 / 05期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

ACCESSORY PROTEINS; CRYSTAL-STRUCTURE; BINDING-PROTEIN; SLIDING CLAMPS; GAMMA-SUBUNIT; HOLOENZYME; REPLICATION; TAU; DELTA; COMPLEX;

D O I：

10.1063/1.4927407

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Several X-ray crystal structures of the E. coli core clamp loader containing the five core (delta('), delta, and three truncated gamma) subunits have been determined, but they lack the psi and chi subunits. We report the first solution structure of the complete seven-subunit clamp loader complex using small angle X-ray scattering. This structure not only provides information about the location of the chi and psi subunits but also provides a model of the dynamic nature of the clamp loader complex. (C) 2015 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License.

引用

页数：8

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