Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
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DOI：
10.1074/jbc.m207796200
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发表时间：
2002-11-29
影响因子：
4.8
通讯作者：
Xia, D
中科院分区：
文献类型：
--
作者：
Guo, FS;Maurizi, MR;Xia, D
大肠杆菌ClpA是一种Hsp100/CLP伴侣蛋白，是依赖于ATP的ClpAP蛋白水解酶的重要组成部分，参与调节蛋白质的降解以及蛋白质聚集体的溶解和降解。ClpA亚基的晶体结构显示了一个具有伪双重对称性的N-末端结构域和两个AAA(+)模块(D1和D2)，每个模块都由一个大亚域和一个小亚域组成，在亚域结合处结合了ADP。N-末端结构域以类似于其他AAA(+)蛋白的接头结合域的方式与D1结构域相互作用。D1和D2是头尾相连的，与蛋白质底物的协同和载体易位一致。在ClpA的平面六聚体模型中，通过将ClpA的D1和D2组装到AAA(+)模块的已知结构的同源六聚体环中，D1-D1和D2-D2界面的差异与它们各自对六聚体稳定性和ATPase活性的贡献有关。
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.