https://scholars.lib.ntu.edu.tw/handle/123456789/641352
標題: | Structural Insights into the Allosteric Operation of the Lon AAA+ Protease | 作者: | Lin, Chien-Chu Su, Shih-Chieh Su, Ming-Yuan PI-HUI LIANG Feng, Chia-Cheng Wu, Shih-Hsiung Chang, Chung-I |
關鍵字: | AAA+ protease; ATPase cycle; LonA; allosteric regulation; crystal structure; pore loops; protein degradation; translocation | 公開日期: | 3-五月-2016 | 卷: | 24 | 期: | 5 | 起(迄)頁: | 667 | 來源出版物: | Structure (London, England : 1993) | 摘要: | The Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation. A hallmark feature shared by AAA+ proteases is the stimulation of ATPase activity by substrates. Here we report the structure of LonA bound to three ADPs, revealing the first AAA+ protease assembly where the six protomers are arranged alternately in nucleotide-free and bound states. Nucleotide binding induces large coordinated movements of conserved pore loops from two pairs of three non-adjacent protomers and shuttling of the proteolytic groove between the ATPase site and a previously unknown Arg paddle. Structural and biochemical evidence supports the roles of the substrate-bound proteolytic groove in allosteric stimulation of ATPase activity and the conserved Arg paddle in driving substrate degradation. Altogether, this work provides a molecular framework for understanding how ATP-dependent chemomechanical movements drive allosteric processes for substrate degradation in a major protein-destruction machine. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/641352 | ISSN: | 09692126 | DOI: | 10.1016/j.str.2016.03.001 |
顯示於: | 藥學系 |
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