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| - | [[Image:4pgm.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:4pgm.png|left|200px]] |
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| | {{STRUCTURE_4pgm| PDB=4pgm | SCENE= }} | | {{STRUCTURE_4pgm| PDB=4pgm | SCENE= }} |
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| - | '''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE'''
| + | ===SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9512715}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9512715 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9512715}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycolytic enzyme]] | | [[Category: Glycolytic enzyme]] |
| | [[Category: Isomerase]] | | [[Category: Isomerase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:28:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:47:21 2008'' |
Revision as of 10:47, 3 July 2008
Template:STRUCTURE 4pgm
SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
Template:ABSTRACT PUBMED 9512715
About this Structure
4PGM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Jul 3 13:47:21 2008
