2JE2

Cytochrome P460 from Nitrosomonas europaea - probable nonphysiological oxidized form

Summary for 2JE2

• Entry DOI: 10.2210/pdb2je2/pdb
• Related: 2JE3
• Descriptor: CYTOCHROME P460, HEME C, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: heme p460, cytochrome p460, cross-linked heme, metal binding protein
• Biological source: NITROSOMONAS EUROPAEA
• Total number of polymer chains: 1
• Total formula weight: 21431.53

Authors

Pearson, A.R.,Elmore, B.O.,Yang, C.,Ferrara, J.D.,Hooper, A.B.,Wilmot, C.M. (deposition date: 2007-01-13, release date: 2007-07-03, Last modification date: 2024-11-06)

Primary citation

Pearson, A.R.,Elmore, B.O.,Yang, C.,Ferrara, J.D.,Hooper, A.B.,Wilmot, C.M.
The Crystal Structure of Cytochrome P460 of Nitrosomonas Europaea Reveals a Novel Cytochrome Fold and Heme-Protein Cross-Link.
Biochemistry, 46:8340-, 2007

PubMed Abstract: 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.

PubMed: 17583915
DOI: 10.1021/BI700086R

Experimental method

X-RAY DIFFRACTION (1.8 Å)