1o08
From Proteopedia
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Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate
Overview
Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.
About this Structure
1O08 is a Single protein structure of sequence from Lactococcus lactis with and as ligands. Active as Beta-phosphoglucomutase, with EC number 5.4.2.6 Full crystallographic information is available from OCA.
Reference
The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction., Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN, Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13. PMID:12637673
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