title: Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa.
abstract: The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) catalyzes the conversion of mannose 6-phosphate to mannose 1-phosphate in the second step of the alginate biosynthetic pathway of Pseudomonas aeruginosa. PMM/PGM has been crystallized by hanging-drop vapor diffusion in space group P2(1)2(1)2(1). Crystals diffract to 1.75 A resolution on a synchrotron X-ray source under cryo-cooling conditions. PMM/PGM substituted with selenomethionine has been purified and crystallizes isomorphously with the native enzyme. Structure determination by MAD phasing is under way. Because of its role in alginate biosynthesis, PMM/PGM is a potential target for therapeutic inhibitors to combat P. aeruginosa infections.
authors.affiliation: Biochemistry Department, University of Missouri, Columbia 65211, USA.
authors.forename: C A
authors.initials: CA
authors.lastname: Regni
authors.forename: P A
authors.initials: PA
authors.lastname: Tipton
authors.forename: L J
authors.initials: LJ
authors.lastname: Beamer
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D009097:Multienzyme Complexes / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000201:enzymology; D010733:Phosphoglucomutase / Q000737:chemistry*; D017875:Phosphotransferases (Phosphomutases) / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011817:Rabbits; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D017875:Phosphotransferases (Phosphomutases); D010733:Phosphoglucomutase; C052799:phosphomannomutase