解解旋酶相关结构域BVU_0683(627-691)的NMR结构为蛋白结构域家族PF03457提供了第一个结构覆盖,表明该结构域与DNA结合。

Jeffrey L Mills, Thomas B Acton, Rong Xiao, John K Everett, Gaetano T Montelione, Thomas Szyperski
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引用次数: 0

摘要

普通拟杆菌(Bacteroides vulgatus) 753个残基蛋白BVU_0683的解旋酶相关(HA)结构域的627-691残基的高质量核磁共振结构显示出全α-螺旋折叠。该结构是HA结构域大蛋白结构域家族PF03457(目前有742个成员)的第一个代表。与结构相似的蛋白质的比较支持HA结构域与DNA结合的假设,并且在构成PF03457的HA结构域家族中,结合特异性差异很大。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Solution NMR structure of the helicase associated domain BVU_0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA.

A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627-691 of the 753-residue protein BVU_0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.

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