2FKM

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

Summary for 2FKM

• Entry DOI: 10.2210/pdb2fkm/pdb
• Related: 1K2Y 1K35 1P5D 1P5G 1PCJ 1PCM 2FKF
• Descriptor: Phosphomannomutase/phosphoglucomutase, 1,6-di-O-phosphono-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• Functional Keywords: alpha/beta protein, enzyme-metal complex, enzyme-ligand complex, isomerase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 50651.68

Authors

Regni, C.A.,Beamer, L.J. (deposition date: 2006-01-04, release date: 2006-04-04, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)