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- Title
The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology.
- Authors
Chow, Sih-Yao; Wang, Yung-Lin; Hsieh, Yu-Chiao; Lee, Guan-Chiun; Liaw, Shwu-Huey
- Abstract
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 of Deinococcus radiodurans TS (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.
- Subjects
TREHALOSE; DEINOCOCCUS radiodurans; BINDING sites
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2017, Vol 73, Issue 11, p588
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X17014303