2je2
CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM
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OverviewOverview
We have determined the 1.8 A X-ray crystal structure of a monoheme c-type, cytochrome, cytochrome P460, from Nitrosomonas europea. The chromophore, possesses unusual spectral properties analogous to those of the catalytic, heme P460 of hydroxylamine oxidoreductase (HAO), the only known heme in, biology to withdraw electrons from an iron-coordinated substrate. The, analysis reveals a homodimeric structure and elucidates a new c-type, cytochrome fold that is predominantly beta-sheet. In addition to the two, cysteine thioether links to the porphyrin typical of c-type hemes, there, is a third proteinaceous link involving a conserved lysine. The covalent, bond is between the lysine side-chain nitrogen and the 13'-meso carbon of, the heme, which, following cross-link formation, is sp3-hybridized, demonstrating the loss of conjugation at this position within the, porphyrin. The structure has implications for the analogous tyrosine-heme, meso carbon cross-link observed in HAO.
About this StructureAbout this Structure
2JE2 is a Single protein structure of sequence from Nitrosomonas europaea with PO4 and HEC as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
The Crystal Structure of Cytochrome P460 of Nitrosomonas europaea Reveals a Novel Cytochrome Fold and Heme-Protein Cross-link(,)., Pearson AR, Elmore BO, Yang C, Ferrara JD, Hooper AB, Wilmot CM, Biochemistry. 2007 Jul 17;46(28):8340-9. Epub 2007 Jun 21. PMID:17583915
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