2WVM

H309A mutant of Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in complex with GDP-alpha-D-Mannose and Mg(II)

Summary for 2WVM

• Entry DOI: 10.2210/pdb2wvm/pdb
• Related: 2WVK 2WVL
• Descriptor: MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE, GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: gt-a fold, transferase, glycosyltransferase, retaining mechanism, glucosyl transferase
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 88622.92

Authors

Goncalves, S.,Borges, N.,Esteves, A.M.,Victor, B.,Soares, C.M.,Santos, H.,Matias, P.M. (deposition date: 2009-10-19, release date: 2010-03-31, Last modification date: 2023-12-20)

Primary citation

Goncalves, S.,Borges, N.,Esteves, A.M.,Victor, B.,Soares, C.M.,Santos, H.,Matias, P.M.
Structural Analysis of Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Synthase Provides Evidence for a Second Catalytic Metal Ion and New Insight Into the Retaining Mechanism of Glycosyltransferases.
J.Biol.Chem., 285:17857-, 2010

PubMed Abstract: Mannosyl-3-phosphoglycerate synthase is a glycosyltransferase involved in the two-step synthetic pathway of mannosylglycerate, a compatible solute that accumulates in response to salt and/or heat stresses in many microorganisms thriving in hot environments. The three-dimensional structure of mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in its binary complex form, with GDP-alpha-D-mannose and Mg(2+), shows a second metal binding site, about 6 A away from the mannose moiety. Kinetic and mutagenesis studies have shown that this metal site plays a role in catalysis. Additionally, Asp(167) in the DXD motif is found within van der Waals contact distance of the C1' atom in the mannopyranose ring, suggesting its action as a catalytic nucleophile, either in the formation of a glycosyl-enzyme intermediate according to the double-displacement S(N)2 reaction mechanism or in the stabilization of the oxocarbenium ion-like intermediate according to the D(N)*A(Nss) (S(N)i-like) reaction mechanism. We propose that either mechanism may occur in retaining glycosyltransferases with a GT-A fold, and, based on the gathered structural information, we identified an extended structural signature toward a common scaffold between the inverting and retaining glycosyltransferases.

PubMed: 20356840
DOI: 10.1074/JBC.M109.095976

Experimental method

X-RAY DIFFRACTION (2.977 Å)