4pgm

File:4pgm.gif

spinqualitylabelsall models 4pgm, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

OverviewOverview

The high resolution crystal structure of Saccharomyces cerevisiae, phosphoglycerate mutase has been determined. This structure shows, important differences from the lower resolution structure deposited in, 1982. The crystal used to determine the new structure was of a different, form, having spacegroup P2(1). The model was refined to a crystallographic, R-factor of 18.9% and a free R-factor of 28.4% using all data between 25, and 2.3 A and employing a bulk solvent correction. The enzyme is a, tetramer of identical, 246 amino acid subunits, whose structure is, revealed to be a dimer of dimers, with four independent active sites, located well away from the subunit contacts. Each subunit contains two, domains, the larger with a typical nucleotide binding fold, although, phosphoglycerate mutase has no physiological requirement to bind, nucleotides. The catalytic-site histidine residues are no longer in a, "clapping-hands" conformation, but more resemble the conformation seen in, the distantly related enzymes prostatic acid phosphatase and, fructose-2,6-bisphosphatase. However, the catalytic histidine residues in, the mutase are found to be much closer to each other than in the, phosphatase structures, perhaps due to the absence of bound ligands in the, mutase crystal. An intricate web of H-bonds is found around the catalytic, histidine residues, high-lighting residues probably important for, maintaining their correct orientation and charge. The positions of certain, other residues, including some found near the catalytic site and some, lining the catalytic-site cleft, have been changed by the correction of, registration errors between sequence and electron density in the original, structure. Electron density was apparent for a portion of the functionally, important C-terminal tail, which was absent from the earlier structure, showing it to adopt a mainly helical conformation.

About this StructureAbout this Structure

4PGM is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Structure known Active Site: CIC. Full crystallographic information is available from OCA.

ReferenceReference

The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase., Rigden DJ, Alexeev D, Phillips SE, Fothergill-Gilmore LA, J Mol Biol. 1998 Feb 20;276(2):449-59. PMID:9512715

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