1BQ4
SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH BENZENE HEXACARBOXYLATE
Summary for 1BQ4
| Entry DOI | 10.2210/pdb1bq4/pdb |
| Descriptor | PROTEIN (PHOSPHOGLYCERATE MUTASE 1), SULFATE ION, BENZENE HEXACARBOXYLIC ACID (3 entities in total) |
| Functional Keywords | isomerase, transferase (phosphoryl), glycolytic enzyme |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 110699.83 |
| Authors | Rigden, D.J.,Phillips, S.E.V.,Fothergill-Gilmore, L.A. (deposition date: 1998-08-20, release date: 1998-08-26, Last modification date: 2023-08-09) |
| Primary citation | Rigden, D.J.,Walter, R.A.,Phillips, S.E.,Fothergill-Gilmore, L.A. Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis. J.Mol.Biol., 289:691-699, 1999 Cited by PubMed Abstract: The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis. PubMed: 10369755DOI: 10.1006/jmbi.1999.2848 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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