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Publication Abstract from PubMed

Glycosyltrehalose synthase (GTSase) converts the glucosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-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 A resolution by X-ray crystallography. The structure of 5389-GTSase can be divided into five domains. The central domain contains the (beta/alpha)8-barrel fold that is conserved as the catalytic domain in the alpha-amylase family. Three invariant catalytic carboxylic amino acids in the alpha-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.

Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389.,Okazaki N, Blaber M, Kuroki R, Tamada T Acta Crystallogr F Struct Biol Commun. 2018 Nov 1;74(Pt 11):741-746. doi:, 10.1107/S2053230X1801453X. Epub 2018 Oct 31. PMID:30387780^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.