2D40
Crystal Structure of Z3393 from Escherichia coli O157:H7
Summary for 2D40
Entry DOI | 10.2210/pdb2d40/pdb |
Descriptor | putative gentisate 1,2-dioxygenase, FE (III) ION (3 entities in total) |
Functional Keywords | gentisic acid, 1, 2-dioxygenase, bicupin, tetramer, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 161141.93 |
Authors | Adams, M.A.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2005-10-05, release date: 2006-09-26, Last modification date: 2024-10-30) |
Primary citation | Adams, M.A.,Singh, V.K.,Keller, B.O.,Jia, Z. Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7 Mol.Microbiol., 61:1469-1484, 2006 Cited by PubMed Abstract: 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. PubMed: 16930152DOI: 10.1111/j.1365-2958.2006.05334.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
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