1dqr | pdb_00001dqr

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE, A GLYCOLYTIC ENZYME THAT MOONLIGHTS AS NEUROLEUKIN, AUTOCRINE MOTILITY FACTOR, AND DIFFERENTIATION MEDIATOR

spinqualitylabelsall models 1dqr, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dqr is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 6PG Activity: Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [G6PI_RABIT] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons (By similarity). 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 The multifunctional protein phosphoglucose isomerase, also known as neuroleukin, autocrine motility factor, and differentiation and maturation mediator, has different roles inside and outside the cell. In the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine. We have determined the three-dimensional structure of rabbit muscle phosphoglucose isomerase complexed with the competitive inhibitor D-gluconate 6-phosphate by X-ray crystallography at 2.5 A resolution. The structure shows that the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit. The location of the bound D-gluconate 6-phosphate inhibitor leads to the identification of residues involved in substrate specificity (Ser209, Ser159, Thr214, Thr217, and Thr211). The results of previously published kinetic studies suggest that a lysine and a histidine are involved in the catalytic mechanism. The crystal structure suggests active site residues Lys518 and His388 might be these residues. In addition, the positions of amino acid residues that are substituted in the genetic disease nonspherocytic hemolytic anemia suggest how these substitutions can result in altered catalysis or protein stability. Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator.,Jeffery CJ, Bahnson BJ, Chien W, Ringe D, Petsko GA Biochemistry. 2000 Feb 8;39(5):955-64. PMID:10653639 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglucoisomerase Phosphoglucose isomerase

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