1tip | pdb_00001tip
From Proteopedia
THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. ReferencesContents | ||||||||||||||||||||||||
This page was last modified 21:22, 29 September 2014.