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首页> 外文期刊>Journal of Molecular Biology >Structural insights into the cryptic DNA-dependent ATPase activity of UvrB.
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Structural insights into the cryptic DNA-dependent ATPase activity of UvrB.

机译：UvrB的隐秘DNA依赖性ATPase活性的结构见解。

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摘要

The UvrABC pathway is a ubiquitously occurring mechanism targeted towards the repair of bulky base damage. Key to this process is UvrB, a DNA-dependent limited helicase that acts as a lesion recognition element whilst part of a tracking complex involving UvrA, and as a DNA-binding platform required for the presentation of damage to UvrC for subsequent processing. We have been able to determine the structure of a ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP. This structure has highlighted the roles of key conserved residues in DNA binding distinct from those of the beta-hairpin, where most of the attention in previous studies has been focussed. We are also the first to report the structural basis underlying conformational re-modelling of the beta-hairpin that is absolutely required for DNA binding and how this event results in an ATPase primed for catalysis. Our data provide the first insights at the molecular level into the transformation of UvrB into an active helicase.
机译：UvrABC途径是针对修复大面积碱基损伤的普遍存在的机制。此过程的关键是UvrB，这是一种依赖于DNA的有限解旋酶，在涉及UvrA的跟踪复合体中，它不仅是病变识别元件，而且是呈递UvrC损伤以进行后续加工所需的DNA结合平台。我们已经能够确定涉及UvrB *（全长UvrB的C端截短），多聚胸腺嘧啶三核苷酸和ADP的三元复合物的结构。这种结构突出了关键的保守残基在DNA结合中的作用，不同于β-发夹的作用，以往研究中的大多数注意力都集中在该基因上。我们也是第一个报告β-发夹构象重塑基础的结构基础，这对于DNA结合是绝对必需的，并且该事件如何导致引发催化的ATPase。我们的数据提供了在分子水平上将UvrB转化为活性解旋酶的初步见解。

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