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2D40

Crystal Structure of Z3393 from Escherichia coli O157:H7

2D40 の概要
エントリーDOI10.2210/pdb2d40/pdb
分子名称putative gentisate 1,2-dioxygenase, FE (III) ION (3 entities in total)
機能のキーワードgentisic acid, 1, 2-dioxygenase, bicupin, tetramer, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, oxidoreductase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数4
化学式量合計161141.93
構造登録者
Adams, M.A.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2005-10-05, 公開日: 2006-09-26, 最終更新日: 2024-10-30)
主引用文献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: 16930152
DOI: 10.1111/j.1365-2958.2006.05334.x
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.41 Å)
構造検証レポート
Validation report summary of 2d40
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-11に公開中

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