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*

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

摘要

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.

原文英語
頁(從 - 到)588-594
頁數7
期刊Acta Crystallographica Section F:Structural Biology Communications
73
發行號11
DOIs
出版狀態已發佈 - 2017 十一月

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 遺傳學
  • 凝聚態物理學

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