2pgi
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THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS
OverviewOverview
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.
About this StructureAbout this Structure
2PGI is a Single protein structure of sequence from Geobacillus stearothermophilus. The following page contains interesting information on the relation of 2PGI with [Aconitase and Iron Regulatory Protein 1]. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
ReferenceReference
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
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