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Structure paper

TitleExpansion of Substrate Specificity and Catalytic Mechanism of Azoreductase by X-ray Crystallography and Site-directed Mutagenesis
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 13889-13896, Year 2008
Publish dateSep 18, 2007 (structure data deposition date)
AuthorsIto, K. / Nakanishi, M. / Lee, W.C. / Zhi, Y. / Sasaki, H. / Zenno, S. / Saigo, K. / Kitade, Y. / Tanokura, M.
External linksJ. Biol. Chem. / PubMed:18337254
MethodsX-ray diffraction
Resolution1.4 - 2.3 Å
Structure data

PDB-2z98:
The crystal structure of AzoR (azoreductase) from Escherichia coli: Oxidized AzoR in tetragonal crystals (The resolution has improved from 1.8 (1v4b) to 1.4 angstrom)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-2z9b:
The crystal structure of AzoR (azoreductase) from Escherichia coli: Reduced AzoR in tetragonal crystals
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2z9c:
The crystal structure of AzoR (azoreductase) from Escherichia coli: AzoR in complex with dicoumarol
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2z9d:
The crystal structure of AzoR (azoreductase) from Escherichia coli: Oxidized AzoR in orthorhombic crystals
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-DTC:
BISHYDROXY[2H-1-BENZOPYRAN-2-ONE,1,2-BENZOPYRONE] / anticoagulant, inhibitor*YM

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / azoreductase / Flavoprotein / FMN / NAD

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