Structural highlights
Function
F261_RAT Synthesis and degradation of fructose 2,6-bisphosphate.
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 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.
Crystal structure of a trapped phosphoenzyme during a catalytic reaction.,Lee YH, Olson TW, Ogata CM, Levitt DG, Banaszak LJ, Lange AJ Nat Struct Biol. 1997 Aug;4(8):615-8. PMID:9253407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee YH, Olson TW, Ogata CM, Levitt DG, Banaszak LJ, Lange AJ. Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nat Struct Biol. 1997 Aug;4(8):615-8. PMID:9253407
