3ZO9

The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis

3ZO9 の概要

• エントリーDOI: 10.2210/pdb3zo9/pdb
• 関連するPDBエントリー: 3ZOA
• 分子名称: TREHALOSE SYNTHASE/AMYLASE TRES, CHLORIDE ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, glycohydrolase, drug design, tuberculosis
• 由来する生物種: MYCOBACTERIUM SMEGMATIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 136921.20

構造登録者

Caner, S.,Nguyen, N.,Aguda, A.,Zhang, R.,Pan, Y.T.,Withers, S.G.,Brayer, G.D. (登録日: 2013-02-21, 公開日: 2013-07-17, 最終更新日: 2023-12-20)

主引用文献

Caner, S.,Nguyen, N.,Aguda, A.,Zhang, R.,Pan, Y.T.,Withers, S.G.,Brayer, G.D.
The Structure of the Mycobacterium Smegmatis Trehalose Synthase Reveals an Unusual Active Site Configuration and Acarbose-Binding Mode.
Glycobiology, 23:1075-, 2013

PubMed Abstract: Trehalose synthase (TreS) catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide. Given the importance of trehalose to survival of mycobacteria, there has been considerable interest in understanding the enzymes involved in its production; indeed the structures of the key enzymes in the other two pathways have already been determined. Herein, we present the first structure of TreS from Mycobacterium smegmatis, thereby providing insights into the catalytic machinery involved in this intriguing intramolecular reaction. This structure, which is of interest both mechanistically and as a potential pharmaceutical target, reveals a narrow and enclosed active site pocket within which intramolecular substrate rearrangements can occur. We also present the structure of a complex of TreS with acarbose, revealing a hitherto unsuspected oligosaccharide-binding site within the C-terminal domain. This may well provide an anchor point for the association of TreS with glycogen, thereby enhancing its role in glycogen biosynthesis and degradation.

PubMed: 23735230
DOI: 10.1093/GLYCOB/CWT044

実験手法

X-RAY DIFFRACTION (1.84 Å)