domain rotation
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Author(s):  
Xudong Wang ◽  
Wenjie Zhao ◽  
Sameer Al-Abdul-Wahid ◽  
Yiming Lu ◽  
Tao Cheng ◽  
...  

2020 ◽  
Vol 840 ◽  
pp. 155680
Author(s):  
Van Quang Nguyen ◽  
Van Thiet Duong ◽  
Thi Huong Nguyen ◽  
Rakwon Kang ◽  
Anh Tuan Pham ◽  
...  

Author(s):  
Liwei Sun ◽  
Ze Yu ◽  
Chunsheng Li ◽  
Wei Liu ◽  
Shusen Wang ◽  
...  

Author(s):  
Sih-Yao Chow ◽  
Yung-Lin Wang ◽  
Yu-Chiao Hsieh ◽  
Guan-Chiun Lee ◽  
Shwu-Huey Liaw

Trehalose synthase (TS) catalyzes the reversible conversion of maltose to trehalose and belongs to glycoside hydrolase family 13 (GH13). Previous mechanistic analysis suggested a rate-limiting protein conformational change, which is probably the opening and closing of the active site. Consistently, crystal structures ofDeinococcus radioduransTS (DrTS) in complex with the inhibitor Tris displayed an enclosed active site for catalysis of the intramoleular isomerization. In this study, the apo structure of the DrTS N253F mutant displays a new open conformation with an empty active site. Analysis of these structures suggests that substrate binding induces a domain rotation to close the active site. Such a substrate-induced domain rotation has also been observed in some other GH13 enzymes.


2016 ◽  
Vol 65 (6) ◽  
pp. 067501
Author(s):  
Yan Bai-Ping ◽  
Zhang Cheng-Ming ◽  
Li Li-Yi ◽  
L Fu-Zai ◽  
Deng Shuang

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Lionel Ballut ◽  
Sébastien Violot ◽  
Santosh Shivakumaraswamy ◽  
Lakshmi Prasoona Thota ◽  
Manu Sathya ◽  
...  

2015 ◽  
Vol 29 (6) ◽  
pp. 1128-1137 ◽  
Author(s):  
Gosan Noh ◽  
Seungjae Bahng ◽  
Youn-Ok Park

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