2fkm
From Proteopedia
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PMM/PGM S108D mutant 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
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
Page seeded by OCA on Wed Nov 21 10:36:27 2007
