The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology

Sih Yao Chow, Yung Lin Wang, Yu Chiao Hsieh, Guan Chiun Lee, Shwu Huey Liaw

Research output: Contribution to journalArticle


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.

Original languageEnglish
Pages (from-to)588-594
Number of pages7
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number11
Publication statusPublished - 2017 Nov



  • X-ray crystallography
  • conformational change
  • domain rotation
  • enzyme mechanism
  • glycoside hydrolase family 13
  • trehalose synthase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Cite this