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首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >ATP-dependent DNA ligase from Archaeoglobus fulgidus displays a tightly closed conformation
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ATP-dependent DNA ligase from Archaeoglobus fulgidus displays a tightly closed conformation

机译：细足古细菌的ATP依赖性DNA连接酶显示出紧密闭合的构象

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摘要

DNA ligases join the breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 3′-hydroxyl and 5′-­phosphate termini. They fall into two classes that require either ATP or NAD+ as the source of an AMP group that is covalently attached to a strictly conserved lysine. Conformational flexibility is essential for the function of multi-domain DNA ligases because they must undergo large conformational changes involving domain rearrangements during the course of the reaction. In the absence of the nicked DNA substrate, both open and closed conformations have been observed for the ATP-dependent DNA ligases from Sulfolobus solfataricus and Pyrococcus furiosus. Here, the crystal structure of an ATP-dependent DNA ligase from Archaeoglobus fulgidus has been determined in the DNA-unbound unadenylated state. It resembles the closed conformation of P. furiosus DNA ligase but was even more closed, thus enhancing our understanding of the conformational variability of these enzymes.
机译：DNA连接酶通过催化相邻3'-羟基和5'-β磷酸末端之间的磷酸二酯键的形成来连接双链DNA的断裂。它们分为两类，它们需要ATP或NAD + 作为共价连接至严格保守的赖氨酸的AMP基团的来源。构象灵活性对于多域DNA连接酶的功能至关重要，因为它们必须在反应过程中经历涉及域重排的大构象变化。在没有刻痕的DNA底物的情况下，已经观察到来自Sulfolobus solfataricus和Pyrococcus furiosus的ATP依赖性DNA连接酶的开放和封闭构象。在这里，已经确定了来自古细菌的ATP依赖性DNA连接酶的晶体结构处于DNA未结合的未腺苷酸化状态。它类似于P.furiosus DNA连接酶的封闭构象，但甚至更为封闭，从而增强了我们对这些酶构象变异性的了解。

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