2d40
Crystal Structure of Z3393 from Escherichia coli O157:H7
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OverviewOverview
Gentisic acid (2,5-dihydroxybenzoic acid) is a key intermediate in aerobic, bacterial pathways that are responsible for the metabolism of a large, number of aromatic compounds. The critical step of these pathways is the, oxygen-dependent reaction catalysed by gentisate 1,2-dioxygenase which, opens the aromatic ring of gentisate to form maleylpyruvate. From gentisic, acid, the cell derives carbon and energy through the conversion of, maleylpyruvate to central metabolites. We have confirmed the annotation of, a gentisate 1,2-dioygenase from the pathogenic O157:H7 Escherichia coli, strain and present the first structural characterization of this family of, enzymes. The identity of the reaction product was revealed using tandem, mass spectroscopy. The operon responsible for the degradation of gentisate, in this organism exhibits a high degree of conservation with the, gentisate-degrading operons of other pathogenic bacteria, including the, Shiga toxin-producing E. coli O103:H2, but does not appear to be present, in non-pathogenic strains. The acquisition of the gentisate operon may, represent a special adaptation to meet carbon source requirements under, conditions of environmental stress and may provide a selective advantage, for enterohaemorrhagic E. coli relative to their non-pathogenic, counterparts.
About this StructureAbout this Structure
2D40 is a Single protein structure of sequence from Escherichia coli o127:h6 with as ligand. Active as Gentisate 1,2-dioxygenase, with EC number 1.13.11.4 Full crystallographic information is available from OCA.
ReferenceReference
Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7., Adams MA, Singh VK, Keller BO, Jia Z, Mol Microbiol. 2006 Sep;61(6):1469-84. Epub 2006 Aug 23. PMID:16930152
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