Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis.
The enzyme phosphoglucosamine mutase catalyzes the conversion of glucosamine 6-phosphate to glucosamine 1-phosphate, an early step in the formation of the nucleotide sugar UDP-N-acetylglucosamine, which is involved in peptidoglycan biosynthesis. These enzymes are part of the large alpha-D-phosphohexomutase enzyme superfamily, but no proteins from the phosphoglucosamine mutase subgroup have been structurally characterized to date. Here, the crystallization of phosphoglucosamine mutase from Bacillus anthracis in space group P3(2)21 by hanging-drop vapor diffusion is reported. The crystals diffracted to 2.7 A resolution under cryocooling conditions. Structure determination by molecular replacement was successful and refinement is under way. The crystal structure of B. anthracis phosphoglucosamine mutase should shed light on the substrate-specificity of these enzymes and will also serve as a template for inhibitor design.
Mehra-Chaudhary
Ritcha
R
Department of Biochemistry, University of Missouri, Columbia, MO 65211, USA.
Neace
Carolyn E
CE
Beamer
Lesa J
LJ
D001408:Bacillus anthracis / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010733:Phosphoglucomutase / Q000737:chemistry*
C097631:phosphoglucosamine mutase; D010733:Phosphoglucomutase