5GT2

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

Summary for 5GT2

• Entry DOI: 10.2210/pdb5gt2/pdb
• Descriptor: Probable deferrochelatase/peroxidase YfeX, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: yfex, dye-decolorizing peroxidase, heme, oxidoreductase
• Biological source: Escherichia coli (strain K12)
• Cellular location: Cytoplasm : P76536
• Total number of polymer chains: 4
• Total formula weight: 139259.70

Authors

Ma, Y.L.,Yuan, Z.G.,Liu, S.,Wang, J.X.,Gu, L.C.,Liu, X.H. (deposition date: 2016-08-18, release date: 2017-02-08, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.093 Å)