2je2: Difference between revisions

Revision as of 15:56, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2je2.png

Template:STRUCTURE 2je2

CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORMCYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM

Template:ABSTRACT PUBMED 17583915

About this StructureAbout this Structure

2JE2 is a Single protein structure of sequence from Nitrosomonas europaea. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM'''
+===CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_17583915}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Heme p460]]
 [[Category: Metal binding protein]]
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