XRAY STRUCTURE DETERMINATION OF RUVB DNA HELICASE

RUVB DNA 解旋酶的 X 射线结构测定

• 批准号: 6586649
• 负责人: CHRISTOPHER D PUTNAM
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586649
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; genome; radiography; structural biology

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.

DNA和RNA解旋酶代表了多种酶， 将核苷酸水解的能量与核酸的解旋耦合， 酸性双螺旋。 这些解旋酶代表了一类重要的 分子马达，其活性对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。 水解ATP的RuvB 解旋酶通过RuvA四聚体靶向假日连接。 总之，这种RuvAB复合物不仅迁移到了 假日连接，但也取代RecA丝从DNA链。 解旋酶是一类古老的酶; 然而，目前还没有这种结构。 我们寻求解决 RuvB作为一类解旋酶的第一个结构，并使用它来 了解ATP水解中涉及的小规模运动是如何 与大规模运动有关。