Journal
FEBS LETTERS
Volume 580, Issue 27, Pages 6338-6342Publisher
WILEY
DOI: 10.1016/j.febslet.2006.10.043
Keywords
cytochrome P450; site-directed mutagenesis; protein folding; Streptomyces
Funding
- NIEHS NIH HHS [ES00267] Funding Source: Medline
- NIGMS NIH HHS [R01 GM071826, R01 GM69970] Funding Source: Medline
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In this work, we have spectroscopically characterised CYP157CI from Streptomyees coelicolor A3(2) which has the motif E(297)QSLW(301) rather than the invariant EXXR motif in the P450 K-helix. Site-directed mutagenesis of native E(297)QSLW(301) in CYP157CI to (EESLR301)-E-297 or E(297)QSRW(301) both containing standard EXXR motifs produced cytochrome P420 proteins thought to be inactive forms of P450 even though wild type CYP157CI has the spectral properties of a normal P450. These results indicate that the EXXR motif is not required in all CYP tertiary architectures and only a single cysteine residue, which coordinates as the fifth thiolate ligand to the P450 haem iron, is invariant in all CYPs structures. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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