Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 apoprotein

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.

Crystallization and Preliminary X-Ray Analysis of Mannosyl-3-Phosphoglycerate Synthase from Thermus Thermophilus Hb27

0.2 M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5, 30-35% MPD WITH 600 MM ZNCL2

MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE FROM THERMUS THERMOPHILUS HB27 IN COMPLEX WITH GDP-ALPHA-D-MANNOSE AND MG(II)

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.

MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE (E.C.2.4.1.217)