5ZCR

DSM5389 glycosyltrehalose synthase

Summary for 5ZCR

• Entry DOI: 10.2210/pdb5zcr/pdb
• Descriptor: Maltooligosyl trehalose synthase, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: trehalose, synthase, hydrolase
• Biological source: Sulfolobus shibatae B12
• Total number of polymer chains: 2
• Total formula weight: 173644.91

Authors

Tamada, T.,Okazaki, N. (deposition date: 2018-02-20, release date: 2018-11-21, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)