Rafferty J B, Sedelnikova S E, Hargreaves D, Artymiuk P J, Baker P J, Sharples G J, Mahdi A A, Lloyd R G, Rice D W
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
Science. 1996 Oct 18;274(5286):415-21. doi: 10.1126/science.274.5286.415.
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.
大肠杆菌DNA结合蛋白RuvA与解旋酶RuvB协同作用，在重组和DNA修复过程中驱动霍利迪中间体的分支迁移。RuvA的原子结构分辨率为1.9埃。RuvA的四个单体以四重对称相关，其方式让人联想到一朵四瓣花。霍利迪连接体的四条DNA双链臂可以模拟成方形平面构型，并对接至围绕中心销的蛋白质凹面的凹槽中，该中心销可能在迁移反应过程中促进链分离。所提出的模型揭示了RuvAB连接体复合物如何也能容纳解离酶RuvC。
