1c7q

THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM

spinqualitylabelsall models 1c7q, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1c7q is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: BE1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G6PI2_GEOSE Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.[HAMAP-Rule:MF_00473] 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 catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase. The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition.,Chou CC, Sun YJ, Meng M, Hsiao CD J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:10770936 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglucose isomerase 3D structures

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