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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8
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Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8

机译：嗜热栖热菌HB8的霍利迪结迁移运动蛋白RuvB的晶体结构

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摘要

We report here the crystal structure of the RuvB motor protein from Thermus thermophds HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive do- mains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition protein RuvA may bind a flexible p-hairpin protruding from the N-terminal domain. The structures of two subunits. related by a noncrystallographic pseudo-2-fold axis, imply that con formational changes of motor protein coupled with ATP hydrolysis may reflect motility essential for its translocation around double-stranded DNA.
机译：我们在这里报告了Thermus thermophds HB8的RuvB运动蛋白的晶体结构，该蛋白在同源重组过程中驱动霍利迪结的分支迁移。 RuvB具有由三个连续域组成的月牙形结构，其中前两个域与ATP结合和水解有关。 DNA很可能与一个大的基本裂口相互作用，该裂口包含ATP结合的口袋和结构域边界，而连接识别蛋白RuvA可能会结合一个从N末端结构域突出的柔性p型发夹。两个亚基的结构。与非晶体伪2倍轴相关，表明运动蛋白的构象变化与ATP水解可能反映了其围绕双链DNA转运所必需的运动性。

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