2pgi | pdb_00002pgi

THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS

spinqualitylabelsall models 2pgi, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pgi is a 1 chain structure with sequence from Geobacillus stearothermophilus. The May 2007 RCSB PDB Molecule of the Month feature on Aconitase and Iron Regulatory Protein 1 by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: PGIB (Geobacillus stearothermophilus) Activity: Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.,Sun YJ, Chou CC, Chen WS, Wu RT, Meng M, Hsiao CD Proc Natl Acad Sci U S A. 1999 May 11;96(10):5412-7. PMID:10318897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglucoisomerase Phosphoglucose isomerase

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