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.The crystal structure of the N253F mutant of trehalose synthase from D. radiodurans reveals a new open conformation with an empty active site, which may provide a snapshot of the apoenzyme prior to substrate binding.
|頁（從 - 到）||588-594|
|期刊||Acta Crystallographica Section F:Structural Biology Communications|
|出版狀態||已發佈 - 2017 11月|
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