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Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas
C A Regni1, P A Tipton, L J Beamer
1Biochemistry Department, University of Missouri, Columbia 65211, USA.
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.