2fkm | pdb_00002fkm
PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound
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Overview
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.
About this Structure
2FKM is a Single protein structure of sequence from Pseudomonas aeruginosa with G16 and ZN as ligands. Active as Phosphomannomutase, with EC number 5.4.2.8 Full crystallographic information is available from OCA.
Reference
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme., Regni C, Schramm AM, Beamer LJ, J Biol Chem. 2006 Jun 2;281(22):15564-71. Epub 2006 Apr 4. PMID:16595672
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