Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LBP

5-chloro-2-hydroxyhydroquinone dehydrochlorinase (TftG) from Burkholderia phenoliruptrix AC1100: Complex with 2,5-dihydroxybenzoquinone

4LBP の概要
エントリーDOI10.2210/pdb4lbp/pdb
関連するPDBエントリー4LBH 4LBI
分子名称5-chloro-2-hydroxyhydroquinone dehydrochlorinase (TftG), 2,5-dihydroxycyclohexa-2,5-diene-1,4-dione (3 entities in total)
機能のキーワードlyase
由来する生物種Burkholderia cepacia
タンパク質・核酸の鎖数1
化学式量合計11462.44
構造登録者
Hayes, R.P.,Lewis, K.M.,Xun, L.,Kang, C. (登録日: 2013-06-20, 公開日: 2013-08-28, 最終更新日: 2024-11-20)
主引用文献Hayes, R.P.,Lewis, K.M.,Xun, L.,Kang, C.
Catalytic Mechanism of 5-Chlorohydroxyhydroquinone Dehydrochlorinase from the YCII Superfamily of Largely Unknown Function.
J.Biol.Chem., 288:28447-28456, 2013
Cited by
PubMed Abstract: TftG, 5-chloro-2-hydroxyhydroquinone (5-CHQ) dehydrochlorinase, is involved in the biodegradation of 2,4,5-trichlorophenoxyacetate by Burkholderia phenoliruptrix AC1100. It belongs to the YCII superfamily, a group of proteins with largely unknown function. In this work, we utilized structural and functional studies, including the apo-form and 2,5-dihydroxybenzoquinone binary complex crystal structures, computational analysis, and site-directed mutagenesis, to determine the dehydrochlorination mechanism. The His-Asp dyad, which initiates catalysis, is strongly conserved in YCII-like proteins. In addition, other catalytically important residues such as Pro-76, which orients the His-Asp catalytic dyad; Arg-17 and Ser-56, which form an oxyanion hole; and Asp-9, which stabilizes the oxyanion hole, are among the most highly conserved residues across the YCII superfamily members. The comprehensive characterization of TftG helps not only for identifying effective mechanisms for chloroaromatic dechlorination but also for understanding the functions of YCII superfamily members, which we propose to be lyases.
PubMed: 23955343
DOI: 10.1074/jbc.M113.499368
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.87 Å)
構造検証レポート
Validation report summary of 4lbp
検証レポート(詳細版)ダウンロードをダウンロード

248942

件を2026-02-11に公開中

PDB statisticsPDBj update infoContact PDBjnumon