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| [[Image:2je2.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2je2| PDB=2je2 | SCENE= }} | | {{STRUCTURE_2je2| PDB=2je2 | SCENE= }} |
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| '''CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM'''
| | ===CYTOCHROME P460 FROM NITROSOMONAS EUROPAEA- PROBABLE NONPHYSIOLOGICAL OXIDIZED FORM=== |
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| ==Overview==
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| 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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17583915 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17583915}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Heme p460]] | | [[Category: Heme p460]] |
| [[Category: Metal binding protein]] | | [[Category: Metal binding protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:45:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:56:45 2008'' |