2FKF

Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound

2FKF の概要

• エントリーDOI: 10.2210/pdb2fkf/pdb
• 関連するPDBエントリー: 1K2Y 1K35 1P5D 1P5G 1PCJ 1PCM
• 分子名称: Phosphomannomutase/phosphoglucomutase, 1,6-di-O-phosphono-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta protein, phosphoserine, enzyme-metal complex, enzyme-ligand 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: 50703.65

構造登録者

Regni, C.A.,Beamer, L.J. (登録日: 2006-01-04, 公開日: 2006-04-04, 最終更新日: 2024-10-16)

主引用文献

Regni, C.,Schramm, A.M.,Beamer, L.J.
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.
J.Biol.Chem., 281:15564-15571, 2006

PubMed Abstract: The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars. The reaction entails two phosphoryl transfers, with an intervening 180 degrees reorientation of the reaction intermediate (e.g. glucose 1,6-bisphosphate) during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is, thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Structural characterization of two PMM/PGM-intermediate complexes with glucose 1,6-bisphosphate provides new insights into the reaction catalyzed by the enzyme, including the reorientation of the intermediate. Kinetic analyses of site-directed mutants prompted by the structural studies reveal active site residues critical for maintaining association with glucose 1,6-bisphosphate during its unique dynamic reorientation in the active site of PMM/PGM.

PubMed: 16595672
DOI: 10.1074/jbc.M600590200

実験手法

X-RAY DIFFRACTION (2 Å)