1K35

Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa

1K35 の概要

• エントリーDOI: 10.2210/pdb1k35/pdb
• 関連するPDBエントリー: 1K2Y
• 分子名称: Phosphomannomutase, ZINC ION (3 entities in total)
• 機能のキーワード: alpha/beta protein, phosphoserine, enzyme-metal complex, isomerase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50870.90

構造登録者

Regni, C.,Tipton, P.A.,Beamer, L.J. (登録日: 2001-10-01, 公開日: 2002-02-13, 最終更新日: 2011-07-13)

主引用文献

Regni, C.,Tipton, P.A.,Beamer, L.J.
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
Structure, 10:269-279, 2002

PubMed Abstract: The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from P. aeruginosa is required for the biosynthesis of two bacterial exopolysaccharides: alginate and lipopolysaccharide (LPS). Both of these molecules play a role in the virulence of P. aeruginosa, an important human pathogen known for its ability to develop antibiotic resistance and cause chronic lung infections in cystic fibrosis patients. The crystal structure of PMM/PGM shows that the enzyme has four domains, three of which have a similar three-dimensional fold. Residues from all four domains of the protein contribute to the formation of a large active site cleft in the center of the molecule. Detailed information on the active site of PMM/PGM lays the foundation for structure-based inhibitor design. Inhibitors of sufficient potency and specificity should impair the biosynthesis of alginate and LPS, and may facilitate clearance of the bacteria by the host immune system and increase the efficacy of conventional antibiotic treatment against chronic P. aeruginosa infections.

PubMed: 11839312
DOI: 10.1016/S0969-2126(02)00705-0

実験手法

X-RAY DIFFRACTION (2.2 Å)