1IAT
CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR
Summary for 1IAT
| Entry DOI | 10.2210/pdb1iat/pdb |
| Related | 1DQR |
| Descriptor | PHOSPHOGLUCOSE ISOMERASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
| Functional Keywords | isomerase, glycolysis enzyme/neurotrophic growth factor/cytokine, two alpha/beta domains |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P06744 |
| Total number of polymer chains | 1 |
| Total formula weight | 63369.00 |
| Authors | Read, J.A.,Pearce, J.,Li, X.,Muirhead, H.,Chirgwin, J.,Davies, C. (deposition date: 2001-03-23, release date: 2001-05-30, Last modification date: 2024-04-03) |
| Primary citation | Read, J.,Pearce, J.,Li, X.,Muirhead, H.,Chirgwin, J.,Davies, C. The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia. J.Mol.Biol., 309:447-463, 2001 Cited by PubMed Abstract: Phosphoglucose isomerase (PGI) is a multifunctional protein, which, inside the cell, functions as a housekeeping enzyme of glycolysis and gluconeogenesis and, outside the cell, exerts wholly unrelated cytokine properties. We have determined the structure of human PGI to a resolution of 1.6 A using X-ray crystallography. The structure is highly similar to other PGIs, especially the architecture of the active site. Fortuitous binding of a sulphate molecule from the crystallisation solution has facilitated an accurate description of the substrate phosphate-binding site. Comparison with both native and inhibitor-bound rabbit PGI structures shows that two loops move closer to the active site upon binding inhibitor. Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change. We suggest a new mechanism for catalysis that uses Glu357 as the base catalyst for the isomerase reaction rather than His388 as proposed previously. The human PGI structure has also provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia. PubMed: 11371164DOI: 10.1006/jmbi.2001.4680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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