title: Crystal structure of a trapped phosphoenzyme during a catalytic reaction.
abstract: The crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water.
authors.forename: Y H
authors.initials: YH
authors.lastname: Lee
authors.forename: T W
authors.initials: TW
authors.lastname: Olson
authors.forename: C M
authors.initials: CM
authors.lastname: Ogata
authors.forename: D G
authors.initials: DG
authors.lastname: Levitt
authors.forename: L J
authors.initials: LJ
authors.lastname: Banaszak
authors.forename: A J
authors.initials: AJ
authors.lastname: Lange
mesh_terms: D000818:Animals; D002384:Catalysis; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005635:Fructosediphosphates / Q000737:chemistry* / Q000378:metabolism; D005636:Fructosephosphates / Q000494:pharmacology; D008099:Liver / Q000201:enzymology; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D025481:Phosphofructokinase-2; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D051381:Rats
chemical_list: D004791:Enzyme Inhibitors; D005635:Fructosediphosphates; D005636:Fructosephosphates; D010750:Phosphoproteins; C027618:fructose-6-phosphate; C027652:fructose 2,6-diphosphate; D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases