XRAY STRUCTURE DETERMINATION OF RUVB DNA HELICASE

DNA和RNA解旋酶代表一类不同的酶 将核苷酸水解的能量与核酸的解离相耦合 酸双螺旋。这些解旋酶代表了一类重要的 分子马达的活动对RNA加工至关重要， 翻译、DNA合成和DNA修复。40 kDa RuvB DNA 解旋酶与DNA修复密切相关。ATP水解型RuvB 解旋酶被Ruva四聚体靶向于假日连接。 总之，这种RuvAB复合体不仅迁移到 假日连接，但也取代了DNA链上的RecA细丝。 整个解旋酶是一类古老的酶； 然而，目前还不存在任何结构。我们寻求解决 RuvB作为一类解旋酶的第一种结构并用于 了解参与三磷酸腺苷水解症的小范围运动 与大规模运动有关。

DNA and RNA helicases represent a diverse class of enzymes that couple the energy of nucleotide hydrolysis to unwinding of nucleic acid double helices. These helicases represent an important class of molecular motors whose activities are critical for RNA processing, translation, DNA synthesis and DNA repair. The 40kDa RuvB DNA helicase is intimately linked to DNA repair. The ATP-hydrolyzing RuvB helicase is targeted to Holiday junctions by the RuvA tetramer. Together, this RuvAB complex not only migrates to branches of the Holiday junctions, but also displaces RecA filament from DNA strands. The entire class of helicases are an ancient class of enzymes; however, no structures currently exist. We seek to solve the structure of RuvB as the first in a class of helicase and use it to understand how small scale movements involved in ATP nydrolysis are linked to large scale motions.