1GZ5

Trehalose-6-phosphate synthase. OtsA

Summary for 1GZ5

• Entry DOI: 10.2210/pdb1gz5/pdb
• Descriptor: ALPHA-TREHALOSE-PHOSPHATE SYNTHASE, URIDINE-5'-DIPHOSPHATE, 6-O-phosphono-alpha-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: trehalose, synthase, glycosyltransferase, rossmann-fold, glucose-6-phosphate, trehalose-6-phosphate
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 4
• Total formula weight: 210418.62

Authors

Gibson, R.P.,Turkenburg, J.P.,Davies, G.J. (deposition date: 2002-05-15, release date: 2003-02-07, Last modification date: 2024-11-06)

Primary citation

Gibson, R.P.,Turkenburg, J.P.,Charnock, S.J.,Lloyd, R.,Davies, G.J.
Insights Into Trehalose Synthesis Provided by the Structure of the Retaining Glycosyltransferase Otsa
Chem.Biol., 9:1337-, 2002

PubMed Abstract: Trehalose is a nonreducing disaccharide that plays a major role in many organisms, most notably in survival and stress responses. In Mycobacterium tuberculosis, it plays a central role as the carbohydrate core of numerous immunogenic glycolipids including "cord factor" (trehalose 6,6'-dimycolate). The classical pathway for trehalose synthesis involves the condensation of UDP-glucose and glucose-6-phosphate to afford trehalose-6-phosphate, catalyzed by the retaining glycosyltransferase OtsA. The configurations of two anomeric positions are set simultaneously, resulting in the formation of a double glycoside. The three-dimensional structure of the Escherichia coli OtsA, in complex with both UDP and glucose-6-phosphate, reveals the active site at the interface of two beta/alpha/beta domains. The overall structure and the intimate details of the catalytic machinery reveal a striking similarity to glycogen phosphorylase, indicating a strong evolutionary link and suggesting a common catalytic mechanism.

PubMed: 12498887
DOI: 10.1016/S1074-5521(02)00292-2

Experimental method

X-RAY DIFFRACTION (2.43 Å)