作者：
Xu, Xiaolong;Wang, Yanhui;Huang, Wei;Li, Danyang;Deng, Zixin;...
通讯作者：
Long, F
作者机构：
Wuhan Univ, Zhongnan Hosp, Sch Pharmaceut Sci, Dept Neurosurg, Wuhan, Peoples R China.
Wuhan Univ, Sch Pharmaceut Sci, Minist Educ, Key Lab Combinatorial Biosynth & Drug Discovery, Wuhan, Peoples R China.
Wuhan Univ, CryoeM Ctr, Wuhan, Peoples R China.
Wuhan Univ, Core Facil, Wuhan, Peoples R China.
通讯机构：
Wuhan Univ, Zhongnan Hosp, Sch Pharmaceut Sci, Dept Neurosurg, Wuhan, Peoples R China.
Wuhan Univ, Sch Pharmaceut Sci, Minist Educ, Key Lab Combinatorial Biosynth & Drug Discovery, Wuhan, Peoples R China.
语种：
英文
关键词：
ClpP protease,AAA+ ATPase,protein degradation,ADEP1,substrate translocation mechanism
期刊：
MBIO
ISSN：
2150-7511
年：
2024
卷：
15
期：
4
页码：
e0003124
基金类别：
MOST | National Key Research and Development Program of China (NKPs)
摘要：
The Clp protease system is important for maintaining proteostasis in bacteria. It consists of ClpP serine proteases and an AAA+ Clp-ATPase such as ClpC1. The hexameric ATPase ClpC1 utilizes the energy of ATP binding and hydrolysis to engage, unfold, and translocate substrates into the proteolytic chamber of homo- or hetero-tetradecameric ClpP for degradation. The assembly between the hetero-tetradecameric ClpP1P2 chamber and the Clp-ATPases containing tandem ATPase domains from the same species has not been studied in depth. Here, we present cryo-EM structures of the substrate-bound ClpC1:shClpP1P2 from Streptomyces hawaiiensis, and shClpP1P2 in complex with ADEP1, a natu...
