Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction

被引：156

作者：

Rafferty, JB

Sedelnikova, SE

Hargreaves, D

Artymiuk, PJ

Baker, PJ

Sharples, GJ

Mahdi, AA

Lloyd, RG

Rice, DW

机构：

[1] UNIV SHEFFIELD, KREBS INST, DEPT MOL BIOL & BIOTECHNOL, SHEFFIELD S10 2TN, S YORKSHIRE, ENGLAND

[2] UNIV NOTTINGHAM, QUEENS MED CTR, DEPT GENET, NOTTINGHAM NG7 2UH, ENGLAND

来源：

SCIENCE | 1996年 / 274卷 / 5286期

基金：

英国惠康基金;

关键词：

D O I：

10.1126/science.274.5286.415

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The Escherichia coli DNA binding protein RuvA acts in concert with the helicase RuvB to drive branch migration of Holliday intermediates during recombination and DNA repair. The atomic structure of RuvA was determined at a resolution of 1.9 angstroms. Four monomers of RuvA are related by fourfold symmetry in a manner reminiscent of a four-petaled flower. The four DNA duplex arms of a Holliday junction can be modeled in a square planar configuration and docked into grooves on the concave surface of the protein around a central pin that may facilitate strand separation during the migration reaction. The model presented reveals how a RuvAB-junction complex may also accommodate the resolvase RuvC.

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页码：415 / 421

页数：7

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