来自热球菌sp. 1519的atp依赖性DNA连接酶显示了OB-fold结构域的新排列。

T Petrova, E Y Bezsudnova, K M Boyko, A V Mardanov, K M Polyakov, V V Volkov, M Kozin, N V Ravin, I G Shabalin, K G Skryabin, T N Stekhanova, M V Kovalchuk, V O Popov
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引用次数: 15

摘要

DNA连接酶通过催化在相邻的5'-磷酸和3'-羟基末端之间形成磷酸二酯键来连接双链DNA中的单链断裂。它们的功能对于在DNA的复制、重组和修复中保持基因组完整性至关重要。高柔性对于DNA连接酶分子的功能是重要的。古菌DNA连接酶的两种类型的整体构象取决于OB折叠结构域的相对位置:闭合构象和开放延伸构象。来自Thermococcus sp.1519(LigTh1519)的ATP依赖性DNA连接酶在结晶状态下的结构以3.02的分辨率测定 Å显示了OB折叠结构域的一种新的相对排列,它位于该结构域在先前确定的古菌DNA连接酶的闭合和开放延伸构象中的位置之间。然而,小角度X射线散射(SAXS)测量表明,在溶液中,LigTh1519分子要么采用开放延伸构象,要么采用中间体和开放延伸构象两者,其中开放延伸构象占主导地位。
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ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.

DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.

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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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