Structural plasticity of the Flp-Holliday junction complex
Structural plasticity of the Flp-Holliday junction complex
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DOI：
10.1016/s0022-2836(02)01370-0
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发表时间：
2003-02-14
影响因子：
5.6
通讯作者：
Rice, PA
中科院分区：
文献类型：
--
作者：
Conway, AB;Chen, Y;Rice, PA
Flp重组酶是λ整合酶或基于酪氨酸的位点特异性重组酶家族的成员，是其催化活性受蛋白质-蛋白质接触调节的酶的有趣实例。它在整个催化循环中表现出一半的活性。Flp在这些重组酶中是独特的，因为它通过催化四聚体内的两个蛋白质单体的相互作用反式组装每个活性位点，其中相互作用对的异构化对于完成完整反应是必不可少的。我们在这里报告的结构的DNA结合的四聚体的Flpe，一种变体的Flp，是更活跃在37 degreesC比野生型重组酶。这种新结构包括第一次观察到的酪氨酸重组酶与入侵的5 '-OH准备攻击共价磷酸酪氨酸残基。与先前确定的Flp结构的比较突出了四聚体中两种类型的蛋白质-蛋白质界面之间的灵活性差异，并更好地定义了这种非常灵活的复合物的构象范围。这些结果表明，空间位阻模型的执行一半的网站活动。(C)2003爱思唯尔科技有限公司版权所有。
The Flp recombinase, a member of the lambda integrase or tyrosine-based family of site-specific recombinases, is an interesting example of an enzyme whose catalytic activity is regulated by protein-protein contacts. It exhibits half-of-the-sites activity throughout its catalytic cycle. Flp is unique among these recombinases, in that it assembles each active site in trans through the interaction of two protein monomers within the catalytic tetramer, with isomerization of interacting pairs being essential to complete a full reaction. We report here the structure of a DNA-bound tetramer of Flpe, a variant of Flp that is more active at 37 degreesC than the wild-type recombinase. This new structure includes the first observation of a tyrosine recombinase with an invading 5'-OH poised to attack the covalent phosphotyrosine residue. Comparison with the previously determined Flp structure highlights differences in flexibility between the two types of protein-protein interfaces in the tetramer and better defines the range of conformations available to this remarkably flexible complex. These results suggest a steric occlusion model for enforcement of half-of-the-sites activity. (C) 2003 Elsevier Science Ltd. All rights reserved.