Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12.
Hexameric glucosamine-6-phosphate deaminase from Escherichia coli has been crystallized isomorphously with both phosphate and ammonium sulphate as precipitants, over a wide pH range (6.0 to 9.0). The crystals belong to space group R32 and the cell parameters in the hexagonal setting are a = b = 125.9 A and c = 223.2 A. A complete native data set was collected to 2.1 A resolution. Self-rotation function studies suggest that the hexamers sit on the 3-fold axis and have point group symmetry 32, with a non-crystallographic dyad relating two monomers linked by an interchain disulfide bridge. A possible packing for the unit cell is proposed.
Horjales
E
E
Instituto de Física e Química de São Carlos, Universidade de São Paulo, Brazil.
Altamirano
M M
MM
Calcagno
M L
ML
Dauter
Z
Z
Wilson
K
K
Garratt
R C
RC
Oliva
G
G
D019747:Aldose-Ketose Isomerases; D000494:Allosteric Regulation / Q000502:physiology; D002238:Carbohydrate Epimerases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D014961:X-Ray Diffraction
C020582:glucosamine-6-phosphate isomerase; D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases