2np9
From Proteopedia
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Crystal structure of a dioxygenase in the Crotonase superfamily
Overview
Enzyme-catalysed oxidations are some of the most common transformations in, primary and secondary metabolism. The vancomycin biosynthetic enzyme DpgC, belongs to a small class of oxygenation enzymes that are not dependent on, an accessory cofactor or metal ion. The detailed mechanism of, cofactor-independent oxygenases has not been established. Here we report, the first structure of an enzyme of this oxygenase class in complex with a, bound substrate mimic. The use of a designed, synthetic substrate analogue, allows unique insights into the chemistry of oxygen activation. The, structure confirms the absence of cofactors, and electron density, consistent with molecular oxygen is present adjacent to the site of, oxidation on the substrate. Molecular oxygen is bound in a small, hydrophobic pocket and the substrate provides the reducing power to, activate oxygen for downstream chemical steps. Our results resolve the, unique and complex chemistry of DpgC, a key enzyme in the biosynthetic, pathway of an important class of antibiotics. Furthermore, mechanistic, parallels exist between DpgC and cofactor-dependent flavoenzymes, providing information regarding the general mechanism of enzymatic oxygen, activation.
About this Structure
2NP9 is a Single protein structure of sequence from Streptomyces toyocaensis with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis., Widboom PF, Fielding EN, Liu Y, Bruner SD, Nature. 2007 May 17;447(7142):342-5. PMID:17507985
Page seeded by OCA on Wed Jan 23 14:58:28 2008
