3bb0
From Proteopedia
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Crystal Structure of a Trapped Phosphate-Intermediate in Vanadium Apochloroperoxidase Catalyzing a Dephosphorylation Reaction
Overview
The crystal structure of the apo form of vanadium chloroperoxidase from, Curvularia inaequalis reacted with para-nitrophenylphosphate was, determined at a resolution of 1.5 A. The aim of this study was to solve, structural details of the dephosphorylation reaction catalyzed by this, enzyme. Since the chloroperoxidase is functionally and evolutionary, related to several acid phosphatases including human glucose-6-phosphatase, and a group of membrane-bound lipid phosphatases, the structure sheds, light on the details of the dephosphorylation catalyzed by these enzymes, as well. The trapped intermediate found is bound to the active site as a, metaphosphate anion PO3-, with its phosphorus atom covalently attached to, the Nepsilon2 atom of His496. An apical water molecule is within, hydrogen-bonding distance to the phosphorus atom of the metaphosphate, and, it is in a perfect position for a nucleophilic attack on the, metaphosphate-histidine intermediate to form the inorganic phosphate. This, is, to our knowledge, the first structural characterization of a real, reaction intermediate of the inorganic phosphate group release in a, dephosphorylation reaction.
About this Structure
3BB0 is a Single protein structure of sequence from Curvularia inaequalis with and as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of a trapped phosphate intermediate in vanadium apochloroperoxidase catalyzing a dephosphorylation reaction., Macedo-Ribeiro S, Renirie R, Wever R, Messerschmidt A, Biochemistry. 2008 Jan 22;47(3):929-34. Epub 2007 Dec 29. PMID:18163651
Page seeded by OCA on Wed Feb 13 08:23:02 2008
