Open AccessCrystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis
Author(s) -
MehraChaudhary Ritcha,
Neace Carolyn E.,
Beamer Lesa J.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109023409
Subject(s) - mutase , bacillus anthracis , crystallization , enzyme , molecular replacement , biochemistry , glucosamine , biosynthesis , chemistry , isomerase , crystallography , stereochemistry , biology , bacteria , organic chemistry , genetics
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 α‐ 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 P 3 2 21 by hanging‐drop vapor diffusion is reported. The crystals diffracted to 2.7 Å 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.