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Structure paper

TitleAzide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta 9 stearoyl-ACP desaturase- implications for oxygen activation and catalytic intermediates.
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 25072-25080, Year 2003
Publish dateMar 7, 2003 (structure data deposition date)
AuthorsMoche, M. / Shanklin, J. / Ghoshal, A. / Lindqvist, Y.
External linksJ. Biol. Chem. / PubMed:12704186
MethodsX-ray diffraction
Resolution2.4 - 3.2 Å
Structure data

PDB-1oq4:
The Crystal Structure of the Complex between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Azide.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1oq7:
The crystal structure of the iron free (Apo-)form of Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-1oq9:
The Crystal Structure of the Complex between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Acetate.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1oqb:
The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-AZI:
AZIDE ION

ChemComp-HOH:
WATER

ChemComp-SR:
STRONTIUM ION

ChemComp-ACT:
ACETATE ION

ChemComp-FE2:
Unknown entry

Source
  • ricinus communis (castor bean)
KeywordsOXIDOREDUCTASE / di-iron enzyme / four-helix bundle / fatty acid biosynthesis / electron transfer

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