2PGI
THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS
Summary for 2PGI
| Entry DOI | 10.2210/pdb2pgi/pdb |
| Descriptor | PHOSPHOGLUCOSE ISOMERASE (2 entities in total) |
| Functional Keywords | phosphoglucose isomerase, autocrinefactor, neuroleukin, motility, glycolysis, isomerase |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm: P13376 |
| Total number of polymer chains | 1 |
| Total formula weight | 50202.76 |
| Authors | Sun, Y.-J.,Chou, C.-C.,Chen, W.-S.,Meng, M.,Hsiao, C.-D. (deposition date: 1998-10-27, release date: 1999-06-15, Last modification date: 2024-02-21) |
| Primary citation | Sun, Y.J.,Chou, C.C.,Chen, W.S.,Wu, R.T.,Meng, M.,Hsiao, C.D. The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin. Proc.Natl.Acad.Sci.USA, 96:5412-5417, 1999 Cited by PubMed Abstract: Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alpha/beta structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity. PubMed: 10318897DOI: 10.1073/pnas.96.10.5412 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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