title: The structure of human phosphoglucose isomerase complexed with a transition-state analogue.
abstract: Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.
authors.affiliation: Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA. davies@musc.edu
authors.forename: Christopher
authors.initials: C
authors.lastname: Davies
authors.forename: Hilary
authors.initials: H
authors.lastname: Muirhead
authors.forename: John
authors.initials: J
authors.lastname: Chirgwin
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005956:Glucose-6-Phosphate Isomerase / Q000737:chemistry*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D014961:X-Ray Diffraction
chemical_list: D008024:Ligands; D005956:Glucose-6-Phosphate Isomerase