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

Research output: Contribution to journal › Article › peer-review

32 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 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\}",

year = "1997",

doi = "10.1038/nsb0897-615",

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journal = "Nature Structural Biology",

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AU - Lee, Y.

AU - Olson, T. W.

AU - Ogata, C. M.

AU - Levitt, David G

AU - Banaszak, L. J.

AU - Lange, Alex J

PY - 1997

Y1 - 1997

N2 - 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.

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.

UR - https://www.scopus.com/pages/publications/0030765355

UR - https://www.scopus.com/pages/publications/0030765355#tab=citedBy

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DO - 10.1038/nsb0897-615

M3 - Article

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AN - SCOPUS:0030765355

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VL - 4

SP - 615

EP - 618

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 8

ER -

Crystal structure of a trapped phosphoenzyme during a catalytic reaction

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