Nature Structural Biology
4, 615 - 618 (1997)
doi:10.1038/nsb0897-615
Crystal structure of a trapped phosphoenzyme during a catalytic reactionYong-Hwan Lee1, Todd W. Olson1, Craig M. Ogata2, David G. Levitt3, Leonard J. Banaszak1, 4
& Alex J. Lange1
1Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota 55455, USA.
2Howard Hughes Medical Institute, Brookhaven National Laboratory, Upton, New York 50648, USA.
3Department of Physiology, University of Minnesota, Minneapolis, Minnesota 55455, USA.
4len_b@dccc.med.umn.edu 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.
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