Crystal structure of a trapped phosphoenzyme during a catalytic reaction

Y. Lee, T. W. Olson, C. M. Ogata, David G Levitt, L. J. Banaszak, Alex J Lange

Research output: Contribution to journalArticle

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)615-618
Number of pages4
JournalNature Structural Biology
Volume4
Issue number8
DOIs
StatePublished - Aug 14 1997

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    Lee, Y., Olson, T. W., Ogata, C. M., Levitt, D. G., Banaszak, L. J., & Lange, A. J. (1997). Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nature Structural Biology, 4(8), 615-618. https://doi.org/10.1038/nsb0897-615