5ZCR

DSM5389 glycosyltrehalose synthase

5ZCR の概要

• エントリーDOI: 10.2210/pdb5zcr/pdb
• 分子名称: Maltooligosyl trehalose synthase, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: trehalose, synthase, hydrolase
• 由来する生物種: Sulfolobus shibatae B12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 173644.91

構造登録者

Tamada, T.,Okazaki, N. (登録日: 2018-02-20, 公開日: 2018-11-21, 最終更新日: 2024-10-09)

主引用文献

Okazaki, N.,Blaber, M.,Kuroki, R.,Tamada, T.
Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389
Acta Crystallogr F Struct Biol Commun, 74:741-746, 2018

PubMed Abstract: Glycosyltrehalose synthase (GTSase) converts the glucosidic bond between the last two glucose residues of amylose from an α-1,4 bond to an α-1,1 bond, generating a nonreducing glycosyl trehaloside, in the first step of the biosynthesis of trehalose. To better understand the structural basis of the catalytic mechanism, the crystal structure of GTSase from the hyperthermophilic archaeon Sulfolobus shibatae DSM5389 (5389-GTSase) has been determined to 2.4 Å resolution by X-ray crystallography. The structure of 5389-GTSase can be divided into five domains. The central domain contains the (β/α)-barrel fold that is conserved as the catalytic domain in the α-amylase family. Three invariant catalytic carboxylic amino acids in the α-amylase family are also found in GTSase at positions Asp241, Glu269 and Asp460 in the catalytic domain. The shape of the catalytic cavity and the pocket size at the bottom of the cavity correspond to the intramolecular transglycosylation mechanism proposed from previous enzymatic studies.

PubMed: 30387780
DOI: 10.1107/S2053230X1801453X

実験手法

X-RAY DIFFRACTION (2.4 Å)