2JE2

Cytochrome P460 from Nitrosomonas europaea - probable nonphysiological oxidized form

2JE2 の概要

• エントリーDOI: 10.2210/pdb2je2/pdb
• 関連するPDBエントリー: 2JE3
• 分子名称: CYTOCHROME P460, HEME C, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: heme p460, cytochrome p460, cross-linked heme, metal binding protein
• 由来する生物種: NITROSOMONAS EUROPAEA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21431.53

構造登録者

Pearson, A.R.,Elmore, B.O.,Yang, C.,Ferrara, J.D.,Hooper, A.B.,Wilmot, C.M. (登録日: 2007-01-13, 公開日: 2007-07-03, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)