Snf2 family ATPases and DExx box helicases:: differences and unifying concepts from high-resolution crystal structures
Snf2 family ATPases and DExx box helicases:: differences and unifying concepts from high-resolution crystal structures
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DOI：
10.1093/nar/gkl540
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发表时间：
2006-09-01
影响因子：
14.9
通讯作者：
Hopfner, Karl-Peter
中科院分区：
文献类型：
--
作者：
Duerr, Harald;Flaus, Andrew;Hopfner, Karl-Peter
与酵母Snf 2蛋白具有序列相似性的蛋白质形成ATP酶的大家族，其作用是改变包括染色质在内的多种DNA-蛋白质结构的结构。Snf 2家族酶在序列上与DExx盒解旋酶相关，但它们不具有解旋酶活性。最近的生物化学和结构研究表明，这些酶的作用机制涉及ATP依赖的DNA易位。晶体结构表明这些酶沿着小沟行进，这是一个可以在重塑过程中产生扭矩或能量的过程。我们回顾了最近的结构和生化研究结果，这表明一个共同的机制基础上的许多两个Snf 2家族和DExx盒解旋酶的行动。
Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA-protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. Recent biochemical and structural studies suggest that the mechanism by which these enzymes act involves ATP-dependent translocation on DNA. Crystal structures suggest that these enzymes travel along the minor groove, a process that can generate the torque or energy in remodelling processes. We review the recent structural and biochemical findings which suggest a common mechanistic basis underlies the action of many of both Snf2 family and DExx box helicases.