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Structure paper

TitleCrystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Journal, issue, pagesJ. Mol. Biol., Vol. 305, Page 851-861, Year 2001
Publish dateFeb 3, 1999 (structure data deposition date)
AuthorsBlodig, W. / Smith, A.T. / Doyle, W.A. / Piontek, K.
External linksJ. Mol. Biol. / PubMed:11162097
MethodsX-ray diffraction
Resolution1.73 - 1.85 Å
Structure data

PDB-1b80:
REC. LIGNIN PEROXIDASE H8 OXIDATIVELY PROCESSED
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

PDB-1b82:
PRISTINE RECOMB. LIGNIN PEROXIDASE H8
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1b85:
LIGNIN PEROXIDASE
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

Source
  • phanerochaete chrysosporium (fungus)
KeywordsOXIDOREDUCTASE / LIGNIN DEGRADATION / HEME / RADICAL REACTION / ELECTRON TRANSFER / AUTOCATALYTIC SELF-OXIDATION / BETA-HYDROXY TRYPTOPHAN / Calcium / Cleavage on pair of basic residues / Disulfide bond / Glycoprotein / Hydrogen peroxide / Iron / Metal-binding / Peroxidase / Zymogen

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