2fkf
From Proteopedia
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Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound
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
2FKF is a Single protein structure of sequence from Pseudomonas aeruginosa with G16 and ZN as ligands. 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
Page seeded by OCA on Wed Nov 21 10:36:09 2007
