The crystal structure of murine p97/VCP at 3.6 Å
The crystal structure of murine p97/VCP at 3.6 Å
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DOI：
10.1016/j.jsb.2003.10.007
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发表时间：
2003-12-01
影响因子：
3
通讯作者：
Freemont, PS
中科院分区：
文献类型：
--
作者：
Huyton, T;Pye, VE;Freemont, PS
p97/VCP是AAA atp酶家族的成员，在膜融合和泛素依赖性蛋白降解中都有作用。在这里，我们展示了3.6埃的小鼠p97晶体结构，其中D2结构域被建模为聚丙氨酸，其余的类似于100个残基缺失。所得到的结构说明了两个p97 AAA结构域在自然六聚体状态下的首尾包装排列，D1结合ADP， D2无核苷酸。在这种结构中观察到的头到尾的包装安排与我们先前预测的尾到尾的包装模型相反。D1和D2结构域之间的连接部分紊乱，表明其具有灵活性。晶体结构的正态分析表明两个AAA畴的反相关运动和不同的构象状态。(C) 2003年Elsevier Inc.出版
p97/VCP is a member of the AAA ATPase family and has roles in both membrane fusion and ubiquitin dependent protein degradation. Here, we present a 3.6 Angstrom crystal structure of murine p97 in which D2 domain has been modelled as poly-alanine and the remaining similar to100 residues are absent. The resulting structure illustrates a head-to-tail packing arrangement of the two p97 AAA domains in a natural hexameric state with D1 ADP bound and D2 nucleotide free. The head-to-tail packing arrangement observed in this structure is in contrast to our previously predicted tail-to-tail packing model. The linker between the D1 and D2 domains is partially disordered, suggesting a flexible nature. Normal mode analysis of the crystal structure suggests anti-correlated motions and distinct conformational states of the two AAA domains. (C) 2003 Published by Elsevier Inc.