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The cytochrome P450 gene family CYP157 does not contain EXXR in the K‐helix reducing the absolute conserved P450 residues to a single cysteine
Author(s) -
Rupasinghe Sanjeewa,
Schuler Mary A.,
Kagawa Norio,
Yuan Hang,
Lei Li,
Zhao Bin,
Kelly Steven L.,
Waterman Michael R.,
Lamb David C.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.043
Subject(s) - cytochrome p450 , cysteine , chemistry , stereochemistry , streptomyces coelicolor , residue (chemistry) , hemeprotein , protein tertiary structure , motif (music) , biochemistry , gene , heme , enzyme , mutant , physics , acoustics
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.