Crystal structure of a trapped phosphoenzyme during a catalytic reaction

Y. Lee, University of Minnesota Twin Cities
T. W. Olson, University of Minnesota Twin Cities
C. M. Ogata, University of Minnesota Twin Cities
D. G. Levitt, University of Minnesota Twin Cities
L. J. Banaszak, University of Minnesota Twin Cities
A. J. Lange, University of Minnesota Twin Cities

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.