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2.4.1.266: glucosyl-3-phosphoglycerate synthase

This is an abbreviated version!
For detailed information about glucosyl-3-phosphoglycerate synthase, go to the full flat file.

Word Map on EC 2.4.1.266

Reaction

NDP-glucose
+
3-phospho-D-glycerate
=
NDP
 +
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate

Synonyms

glucosyl-3-phosphoglycerate synthase, glucosyl-3-phosphoglycerate synthase/phosphatase, glucosylphosphoglycerate synthase, GpgS, GpgS protein, GpgS/P, More, MSMEG_5084, RB1005, Rv1208 protein

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.266 glucosyl-3-phosphoglycerate synthase

Crystallization

Crystallization on EC 2.4.1.266 - glucosyl-3-phosphoglycerate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor forms a native ternary complex. The catalytic mechanism is a front-side substrate-assisted SNi-type reaction
hanging-drop vapour diffusion method at 20°C, three-dimensional structure of the apoenzyme, as well as of its ternary complex with UDP and 3-phosphoglycerate is determined by X-ray crystallography, to a resolution of 2.5 and 2.7 A, respectively
-
structures of the unliganded form and in binary and ternary complexes with substrates. The L loop located in the active site adopts open and closed states. Both states coexist, but the conformational equilibrium is highly displaced to the open conformation. Both phosphoglycerate and UDP-Glc-Mn2+ can separately bind to the GpgS structure. Phosphoglycerate binds to a positively charged pocket located in the C-terminal domain of the enzyme, with the L loop displaying a closed conformation. UDP-Glc binds to a positively charged pocket mainly located in the N-terminal of the enzyme, with the alpha- and beta-phosphates coordinating the metal cofactor Mn2+. Following the reaction, glucosylphosphoglycerate is first released with the assistance of the highly disordered Loop 165-184