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Crystal structure of a trapped phosphoenzyme during a catalytic reaction

Nature Structural Biology volume 4, pages 615–618 (1997)Cite this article

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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Authors and Affiliations

  1. Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    Yong-Hwan Lee, Todd W. Olson, Leonard J. Banaszak & Alex J. Lange

  2. Howard Hughes Medical Institute, Brookhaven National Laboratory, Upton, New York, 50648, USA

    Craig M. Ogata

  3. Department of Physiology, University of Minnesota, Minneapolis, Minnesota, 55455, USA

    David G. Levitt

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  6. Alex J. Lange
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Lee, YH., Olson, T., Ogata, C. et al. Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nat Struct Mol Biol 4, 615–618 (1997). https://doi.org/10.1038/nsb0897-615

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