EC Number   |
|---|
    2.4.1.266 | 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 |
| 2.4.1.266 | 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 |
| 2.4.1.266 | 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 |
