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TitleA Single Mutation in Cytochrome P450 BM3 Induces the Conformational Rearrangement Seen upon Substrate Binding in the Wild-type Enzyme
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 23287-23293, Year 2004
Publish dateMar 9, 2004 (structure data deposition date)
AuthorsJoyce, M.G. / Girvan, H.M. / Munro, A.W. / Leys, D.
External linksJ. Biol. Chem. / PubMed:15020590
MethodsX-ray diffraction
Resolution2 - 2.75 Å
Structure data

PDB-1smi:
A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1smj:
Structure of the A264E mutant of cytochrome P450 BM3 complexed with palmitoleate
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

ChemComp-PAM:
PALMITOLEIC ACID

Source
  • bacillus megaterium (bacteria)
KeywordsOXIDOREDUCTASE / monooxygenase; fatty acid oxygenase; cytochrome P450; substrate binding / monooxygenase; fatty acid oxygenase; cytochrome P450; substrate binding; palmitoleate

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