5YKB

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

Replaces:  5GTV

Summary for 5YKB

• Entry DOI: 10.2210/pdb5ykb/pdb
• Related: 4TVU
• Descriptor: Trehalose synthase, CALCIUM ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: trehalose synthase, glycoside hydrolase family 13, isomerase
• Biological source: Deinococcus radiodurans str. R1
• Total number of polymer chains: 4
• Total formula weight: 260341.19

Authors

Chow, S.Y.,Hsieh, Y.C.,Liaw, S.H. (deposition date: 2017-10-13, release date: 2017-10-25, Last modification date: 2023-11-22)

Primary citation

Chow, S.Y.,Wang, Y.L.,Hsieh, Y.C.,Lee, G.C.,Liaw, S.H.
The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology
Acta Crystallogr F Struct Biol Commun, 73:588-594, 2017

PubMed 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.

PubMed: 29095151
DOI: 10.1107/S2053230X17014303

Experimental method

X-RAY DIFFRACTION (2.76 Å)