Structural Insights into the Allosteric Operation of the Lon AAA+ Protease
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- 作者：Chien-Chu Lin1 ; 2 ; 5 ; Shih-Chieh Su1 ; 3 ; 5 ; Ming-Yuan Su1 ; Pi-Hui Liang4 ; Chia-Cheng Feng1 ; Shih-Hsiung Wu1 ; 3 ; Chung-I Chang1 ; 3 ; chungi@gate.sinica.edu.tw" class="auth_mail" title="E-mail the corresponding author
- 关键词：AAA+ protease ; LonA ; pore loops ; translocation ; ATPase cycle ; allosteric regulation ; protein degradation ; crystal structure
- 刊名：Structure
- 出版年：2016
- 出版时间：3 May 2016
- 年：2016
- 卷：24
- 期：5
- 页码：667-675
- 全文大小：3662 K
文摘
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First structure of a hexameric AAA+ protease assembly bound to three ADPs
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The six protomers are arranged alternately in nucleotide-free and bound states
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Pore loops from two pairs of three non-adjacent protomers move cooperatively
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Occupied substrate-binding groove forms the allosteric site for ATPase stimulation