The cytochrome P450 gene family CYP157 does not contain EXXR in the K-helix reducing the absolute conserved P450 residues to a single cysteine.

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 Lett

journal_title

FEBS letters

authors

Rupasinghe S,Schuler MA,Kagawa N,Yuan H,Lei L,Zhao B,Kelly SL,Waterman MR,Lamb DC

doi

10.1016/j.febslet.2006.10.043

subject

Has Abstract

pub_date

2006-11-27 00:00:00

pages

6338-42

issue

27

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01258-0

journal_volume

580

pub_type

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