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

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.

Source: Acta Crystallographica Section F - October 20, 2017 Category: Biochemistry Authors: Chow, S.-Y. Wang, Y.-L. Hsieh, Y.-C. Lee, G.-C. Liaw, S.-H. Tags: trehalose synthase glycoside hydrolase family 13 enzyme mechanism conformational change domain rotation X-ray crystallography research communications Source Type: research