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TitleThe catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
Journal, issue, pagesFebs J., Vol. 278, Page 2387-2394, Year 2011
Publish dateSep 30, 2005 (structure data deposition date)
AuthorsYoshida, T. / Tsuge, H. / Konno, H. / Hisabori, T. / Sugano, Y.
External linksFebs J. / PubMed:21569205
MethodsX-ray diffraction
Resolution1.4 - 2.8 Å
Structure data

PDB-2d3q:
Crystal Structure of a Decolorizing Peroxidase (DyP) That Catalyses the Biological Oxidation of Anthraquinone Derivatives
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3afv:
Dye-decolorizing peroxidase (DyP) at 1.4 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3mm1:
Dye-decolorizing peroxidase (DyP) D171N
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-3mm2:
Dye-decolorizing peroxidase (DyP) in complex with cyanide
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-3mm3:
Dye-decolorizing peroxidase (DyP) D171N in complex with cyanide
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CYN:
CYANIDE ION

Source
  • bjerkandera adusta (fungus)
KeywordsOXIDOREDUCTASE / strands and helix / dyp / dye-decolorizing peroxidase / beta barrel / aspartic acid

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