Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa

Authors
Regni, CA Tipton, PA Beamer, LJ
Citation
Ca. Regni et al., Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa, ACT CRYST D, 56, 2000, pp. 761-762
Citations number
7
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
6
Pages
761 - 762
Database
ISI
SICI code
0907-4449(200006)56:<761:CAICAO>2.0.ZU;2-M
Abstract
The enzyme phosphomannomutase/phosphoglucomutase (PMM/ PGM) catalyzes the c onversion 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 Angstrom resolution on a synchrotron X-ray source under cryo-cooling conditions. PMM/PGM substituted with selenomethio nine has been purified and crystallizes isomorphously with the native enzym e. Structure determination by MAD phasing is under way. Because of its role in alginate biosynthesis, PMM/PGM is a potential target for therapeutic in hibitors to combat P. aeruginosa infections.