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Crystal structure of a trapped phosphoenzyme during a catalytic reaction.
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.
PMID: 9253407 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
Watkins HA, Baker EN.
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[J Bacteriol. 2006]
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Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism.
Monedero V, Poncet S, Mijakovic I, Fieulaine S, Dossonnet V, Martin-Verstraete I, Nessler S, Deutscher J.
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[EMBO J. 2001]
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Snapshot of a phosphorylated substrate intermediate by kinetic crystallography.
Käck H, Gibson KJ, Lindqvist Y, Schneider G.
Proc Natl Acad Sci U S A. 1998 May 12; 95(10):5495-500.
[Proc Natl Acad Sci U S A. 1998]
Structures reported by this article