5GT2

Crystal Structure and Biochemical Features of dye-decolorizing peroxidase YfeX from Escherichia coli O157

5GT2 の概要

• エントリーDOI: 10.2210/pdb5gt2/pdb
• 分子名称: Probable deferrochelatase/peroxidase YfeX, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: yfex, dye-decolorizing peroxidase, heme, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cytoplasm : P76536
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139259.70

構造登録者

Ma, Y.L.,Yuan, Z.G.,Liu, S.,Wang, J.X.,Gu, L.C.,Liu, X.H. (登録日: 2016-08-18, 公開日: 2017-02-08, 最終更新日: 2024-03-20)

主引用文献

Liu, X.,Yuan, Z.,Wang, J.,Cui, Y.,Liu, S.,Ma, Y.,Gu, L.,Xu, S.
Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp(143) and Arg(232) play divergent roles toward different substrates
Biochem. Biophys. Res. Commun., 484:40-44, 2017

PubMed Abstract: YfeX from Escherichia coli O157 is a bacterial dye-decolorizing peroxidase that represents both dye-decoloring activity and typical peroxidase activity. We reported the crystal structure of YfeX bound to heme at 2.09 Å resolution. The YfeX monomer resembles a ferredoxin-like fold and contains two domains. The three conserved residues surrounding the heme group are His, Asp and Arg. His functions as the proximal axial ligand of the heme iron atom. Biochemical data show that the catalytic significance of the conserved Asp and Arg depends on the substrate types and that YfeX may adopt various catalytic mechanisms toward divergent substrates. In addition, it is observed that an access tunnel spans from the protein molecular surface to the heme distal region, it serves as the passageway for the entrance and binding of the HO.

PubMed: 28109884
DOI: 10.1016/j.bbrc.2017.01.081

実験手法

X-RAY DIFFRACTION (2.093 Å)