Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
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DOI：
10.1016/j.jsb.2003.11.008
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发表时间：
2004-04-01
影响因子：
3
通讯作者：
Wilkinson, AJ
中科院分区：
文献类型：
--
作者：
Ogura, T;Whiteheart, SW;Wilkinson, AJ
精氨酸是AAA和AAA（+）蛋白的ATP酶结构域的活性位点和亚基界面的重复特征。在特定的家族成员中，这些残基占据ATP辅因子附近的四个关键位点中的两个或更多个，在那里它们将ATP结合和水解的化学事件转化为机械化学结果。结构和生物化学分析已经导致这些保守的蛋白质发挥关键作用的分子机制的建议。然而，比较研究指出，这些保守的caseine的功能分歧。在这篇综述中，我们将讨论什么是已知的这些关键的精氨酸和什么可以得出结论，他们在AAA和AAA（+）蛋白质的功能的作用。(C)2003爱思唯尔公司All rights reserved.
Arginines are a recurrent feature of the active sites and subunit interfaces of the ATPase domains of AAA and AAA(+) proteins. In particular family members these residues occupy two or more, of four key sites in the vicinity of the ATP cofactor, where they transduce the chemical events of ATP binding and hydrolysis into a mechanochemical outcome. Structural and biochemical analyses have led to the proposal of molecular mechanisms in which these conserved arginines play crucial roles. Comparative studies, however, point to functional divergence for each of these conserved arginines. In this review, we will discuss what is known about these critical arginines and what can be concluded about their role in the function of AAA and AAA(+) proteins. (C) 2003 Elsevier Inc. All rights reserved.