5YKB

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

「5GTV」から置き換えられました

5YKB の概要

• エントリーDOI: 10.2210/pdb5ykb/pdb
• 関連するPDBエントリー: 4TVU
• 分子名称: Trehalose synthase, CALCIUM ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: trehalose synthase, glycoside hydrolase family 13, isomerase
• 由来する生物種: Deinococcus radiodurans str. R1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 260341.19

構造登録者

Chow, S.Y.,Hsieh, Y.C.,Liaw, S.H. (登録日: 2017-10-13, 公開日: 2017-10-25, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.76 Å)