Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy.
Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy.
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DOI：
10.1098/rsob.130142
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发表时间：
2014-03-05
期刊：
影响因子：
5.8
通讯作者：
Freemont PS
中科院分区：
文献类型：
--
作者：
Yeung HO;Förster A;Bebeacua C;Niwa H;Ewens C;McKeown C;Zhang X;Freemont PS
II型AAA+蛋白p97参与许多细胞活动，包括内质网相关降解、转录激活、膜融合和细胞周期控制。这些活性至少部分受到泛素系统的调控，其中p97被认为针对大分子复合物中的泛素化蛋白底物，并协助其提取或拆卸。尽管ATP酶活性对p97的功能至关重要，但对于ATP结合或水解如何与p97构象变化和底物重塑相结合，我们知之甚少。在这里，我们使用单粒子电子冷冻显微镜（cryo-EM）研究核苷酸对p97构象的影响。我们已经确定了在低温电镜数据集中的构象异质性，从中我们已经解决了两个主要的p97构象。构象的比较揭示了核苷酸结合和水解时的环间旋转可能与靶蛋白复合物的重塑有关。
The type II AAA+ protein p97 is involved in numerous cellular activities, including endoplasmic reticulum-associated degradation, transcription activation, membrane fusion and cell-cycle control. These activities are at least in part regulated by the ubiquitin system, in which p97 is thought to target ubiquitylated protein substrates within macromolecular complexes and assist in their extraction or disassembly. Although ATPase activity is essential for p97 function, little is known about how ATP binding or hydrolysis is coupled with p97 conformational changes and substrate remodelling. Here, we have used single-particle electron cryomicroscopy (cryo-EM) to study the effect of nucleotides on p97 conformation. We have identified conformational heterogeneity within the cryo-EM datasets from which we have resolved two major p97 conformations. A comparison of conformations reveals inter-ring rotations upon nucleotide binding and hydrolysis that may be linked to the remodelling of target protein complexes.
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影响因子：
2.2
作者：
VANHEEL, M
通讯作者：
VANHEEL, M
DOI：
10.1038/nsb972
发表时间：
2003-10-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
DeLaBarre, B;Brunger, AT
通讯作者：
Brunger, AT
影响因子：
5.6
作者：
Beuron, F;Flynn, TC;Freemont, PS
通讯作者：
Freemont, PS
影响因子：
3
作者：
Huyton, T;Pye, VE;Freemont, PS
通讯作者：
Freemont, PS
影响因子：
3.3
作者：
Dalal, S;Rosser, MFN;Hanson, PI
通讯作者：
Hanson, PI