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首页> 外文期刊>Journal of Molecular Biology >Solution NMR studies of Chlorella virus DNA ligase-adenylate.
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Solution NMR studies of Chlorella virus DNA ligase-adenylate.

机译：小球藻病毒DNA连接酶-腺苷酸的溶液NMR研究。

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摘要

DNA ligases are essential guardians of genome integrity by virtue of their ability to recognize and seal 3'-OH/5'-phosphate nicks in duplex DNA. The substrate binding and three chemical steps of the ligation pathway are coupled to global and local changes in ligase structure, involving both massive protein domain movements and subtle remodeling of atomic contacts in the active site. Here we applied solution NMR spectroscopy to study the conformational dynamics of the Chlorella virus DNA ligase (ChVLig), a minimized eukaryal ATP-dependent ligase consisting of nucleotidyltransferase, OB, and latch domains. Our analysis of backbone (15)N spin relaxation and (15)N,(1)H residual dipolar couplings of the covalent ChVLig-AMP intermediate revealed conformational sampling on fast (picosecond to nanosecond) and slow timescales (microsecond to millisecond), indicative of interdomain and intradomain flexibility. We identified local and global changes in ChVLig-AMP structure and dynamics induced by phosphate. In particular, the chemical shift perturbations elicited by phosphate were clustered in the peptide motifs that comprise the active site. We hypothesize that phosphate anion mimics some of the conformational transitions that occur when ligase-adenylate interacts with the nick 5'-phosphate.
机译：DNA连接酶凭借其识别和密封双链DNA中3'-OH / 5'-磷酸刻痕的能力，是基因组完整性的重要守护者。底物结合和连接途径的三个化学步骤与连接酶结构的整体和局部变化相关，涉及大量蛋白质结构域移动和活性位点中原子接触的细微重塑。在这里，我们应用溶液NMR光谱研究小球藻病毒DNA连接酶（ChVLig）的构象动力学，这是一种最小的由核糖基转移酶，OB和闩锁结构域组成的，依赖真核的ATP依赖性连接酶。我们对共价ChVLig-AMP中间体的骨架（15）N自旋弛豫和（15）N，（1）H残留偶极偶合的分析表明，在快速（皮秒至纳秒）和慢速时间段（微秒至毫秒）上进行构象采样跨域和域内灵活性。我们确定了ChVLig-AMP结构和磷酸盐诱导的动力学的局部和全局变化。特别地，由磷酸盐引起的化学位移扰动聚集在包含活性位点的肽基序中。我们假设磷酸根阴离子模拟当连接酶-腺苷酸与5'-磷酸切口相互作用时发生的一些构象转变。

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