1O03

Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate

Summary for 1O03

• Entry DOI: 10.2210/pdb1o03/pdb
• Related: 1LVH 1O08
• Descriptor: beta-phosphoglucomutase, 1,6-di-O-phosphono-alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: haloacid dehalogenase superfamily, phosphotransferase, pentavalent phosphate intermediate, isomerase
• Biological source: Lactococcus lactis
• Total number of polymer chains: 1
• Total formula weight: 24603.01

Authors

Lahiri, S.D.,Zhang, G.,Dunaway-Mariano, D.,Allen, K.N. (deposition date: 2003-02-20, release date: 2003-03-18, Last modification date: 2024-04-03)

Primary citation

Lahiri, S.D.,Zhang, G.,Dunaway-Mariano, D.,Allen, K.N.
The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction.
Science, 299:2067-2071, 2003

PubMed Abstract: 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.

PubMed: 12637673
DOI: 10.1126/science.1082710

Experimental method

X-RAY DIFFRACTION (1.4 Å)