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

doi:10.1038/nsb0897-615

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

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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 language	English (US)
Pages (from-to)	615-618
Number of pages	4
Journal	Nature Structural Biology
Volume	4
Issue number	8
DOIs	https://doi.org/10.1038/nsb0897-615
State	Published - 1997

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title = "Crystal structure of a trapped phosphoenzyme during a catalytic reaction",

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.",

author = "Y. Lee and Olson, {T. W.} and Ogata, {C. M.} and Levitt, {David G} and Banaszak, {L. J.} and Lange, {Alex J}",

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AU - Levitt, David G

AU - Banaszak, L. J.

AU - Lange, Alex J

PY - 1997

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AB - 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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Crystal structure of a trapped phosphoenzyme during a catalytic reaction

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