Abstract:
:In this work, we have spectroscopically characterised CYP157C1 from Streptomyces 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 CYP157C1 to E(297)ESLR(301) 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 CYP157C1 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Rupasinghe S,Schuler MA,Kagawa N,Yuan H,Lei L,Zhao B,Kelly SL,Waterman MR,Lamb DCdoi
10.1016/j.febslet.2006.10.043subject
Has Abstractpub_date
2006-11-27 00:00:00pages
6338-42issue
27eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01258-0journal_volume
580pub_type
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