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首页> 外文期刊>Structure >The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold
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The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold

机译：大肠杆菌RusA核酸内切酶的结构揭示了新的霍利迪结DNA结合折叠

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Holliday junction resolution performed by a variety of structure-specific endonucleases is a key step in DNA recombination and repair. It is believed that all resolvases carry out their reaction chemistries in a similar fashion, utilizing a divalent cation to facilitate the hydrolysis of the phosphodiester backbone of the DNA, but their architecture varies. To date, with the exception of bacteriophage T4 endonuclease VII, each of the known resolvase enzyme structures has been categorized into one of two families: the integrases and the nucleases. We have now determined the structure of the Escherichia coli RusA Holliday junction resolvase, which reveals a fourth structural class for these enzymes. The structure suggests that dimer formation is essential for Mg2+ cation binding and hence catalysis and that like the other resolvases, RusA distorts its Holliday junction target upon binding. Key residues identified by mutagenesis experiments are well positioned to interact with the DNA. [References: 56]
机译：通过各种结构特异性核酸内切酶进行的霍利迪连接解析是DNA重组和修复的关键步骤。据信，所有的拆分物以相似的方式进行其反应化学，利用二价阳离子促进DNA的磷酸二酯主链的水解，但是它们的结构变化。迄今为止，除噬菌体T4核酸内切酶VII外，每个已知的分辨酶结构均归为两个家族之一：整合酶和核酸酶。现在，我们已经确定了大肠杆菌RusA Holliday连接解析酶的结构，该结构揭示了这些酶的第四类结构。该结构表明，二聚体的形成对于Mg2 +阳离子的结合至关重要，因此对于催化是必不可少的，并且与其他拆分物一样，RusA在结合时会扭曲其霍利迪连接靶。通过诱变实验确定的关键残基处于与DNA相互作用的良好位置。 [参考：56]

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