2je2 | pdb_00002je2

Cytochrome P460 from Nitrosomonas europaea - probable nonphysiological oxidized form

spinqualitylabelsall models 2je2, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2je2 is a 1 chain structure with sequence from "bacterium_nitrosomonas"_lehmann_and_neumann_1899 "bacterium nitrosomonas" lehmann and neumann 1899. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEC, PO4 Related: 2je3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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