Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase
Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase
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DOI：
10.1016/s0969-2126(00)00101-5
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发表时间：
2000-03-15
期刊：
影响因子：
5.7
通讯作者：
Wigley, DB
中科院分区：
文献类型：
--
作者：
Pan, H;Wigley, DB
背景：DNA引物酶催化DNA聚合酶复制DNA所需的短RNA引物的合成。引物酶包括三个功能域：锌结合结构域，负责模板识别，聚合酶结构域，和一个域，与复制解旋酶，DnaB.Results相互作用：我们提出的晶体结构的锌结合结构域的DNA引物酶嗜热脂肪芽孢杆菌，确定在1.7埃分辨率。这是关于任何DNA引发酶的第一个高分辨率结构信息。讨论了该结构域与单链DNA template.Conclusions相互作用的模型：DNA引物酶锌结合结构域的结构证实了该蛋白属于锌带亚家族。与其他核酸结合蛋白的结构比较表明，引发酶的β片层可能是DNA结合表面，该表面上的保守残基参与DNA的结合和识别。
Background: DNA primases catalyse the synthesis of the short RNA primers that are required for DNA replication by DNA polymerases. Primases comprise three functional domains: a zinc-binding domain that is responsible for template recognition, a polymerase domain, and a domain that interacts with the replicative helicase, DnaB.Results: We present the crystal structure of the zinc-binding domain of DNA primase from Bacillus stearothermophilus, determined at 1.7 Angstrom resolution. This is the first high-resolution structural information about any DNA primase. A model is discussed for the interaction of this domain with the single-stranded DNA template.Conclusions: The structure of the DNA primase zinc-binding domain confirms that the protein belongs to the zinc ribbon subfamily. Structural comparison with other nucleic acid binding proteins suggests that the beta sheet of primase is likely to be the DNA-binding surface, with conserved residues on this surface being involved in the binding and recognition of DNA.