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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >The 1.58 angstrom resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding
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The 1.58 angstrom resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

机译:噬菌体SF6小末端酶DNA结合结构域的1.58埃解析结构为DNA结合提供了新的提示

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摘要

DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1P with the packaging-initiation site to be proposed.
机译:尾部噬菌体和进化相关疱疹病毒中的DNA包装受病毒编码的末端酶控制。与许多其他噬菌体一样,在枯草芽孢杆菌噬菌体SF6和SPP1中,末端酶复合物由两种蛋白质组成:G1P和G2P。据报道,噬菌体SF6小末端酶亚基G1P的N末端DNA结合结构域的晶体结构。与其他DNA结合蛋白的结构比较允许提出G1P与包装起始位点相互作用的通用模型。

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