噬菌体SF6小末端酶DNA结合结构域分辨率为1.58 Å的结构为DNA结合提供了新线索。
The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.
作者信息
Benini Stefano, Chechik Maria, Ortiz Lombardía Miguel, Polier Sigrun, Leech Andrew, Shevtsov Mikhail B, Alonso Juan C
机构信息
Laboratory of Bioorganic Chemistry and Crystallography, Faculty of Science and Technology, Free University of Bolzano, Piazza Università 5, 39100 Bolzano, Italy.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):376-81. doi: 10.1107/S1744309113004399. Epub 2013 Mar 28.
Abstract
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.
摘要
有尾噬菌体以及进化相关疱疹病毒中的DNA包装由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。本文报道了噬菌体SF6小末端酶亚基G1P的N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，有助于提出G1P与包装起始位点相互作用的通用模型。
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