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1ehf

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[[Image:1ehf.gif|left|200px]]
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{{Seed}}
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[[Image:1ehf.png|left|200px]]
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{{STRUCTURE_1ehf| PDB=1ehf | SCENE= }}
{{STRUCTURE_1ehf| PDB=1ehf | SCENE= }}
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'''CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S'''
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===CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S===
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==Overview==
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Cytochrome P450nor (P450nor) is a heme enzyme isolated from the denitrifying fungus Fusarium oxysporum and catalyzes the NO reduction to N2O. Crystal structures of the wild type and two Ser286 mutants (Ser286--&gt;Val, Ser286--&gt;Thr) of P450nor have been determined for the ferric resting forms at a 1.7 A resolution at cryogenic temperature (100 K). We carried out three comparative analyses: (1) between the structures of P450nor at room temperature and cryogenic temperature, (2) between the structures of P450nor and four monooxygenase P450s, and (3) between the structures of the WT and the Ser286 mutant enzymes of P450nor. Comparison of the charge distribution on the protein surface suggests that proton and electron flow to the heme site is quite different in P450nor than in monooxygenase P450s. On the basis of the mutant structures, it was found that a special hydrogen-bonding network, Wat99-Ser286-Wat39-Asp393-solvent, acts as a proton delivery pathway in NO reduction by P450nor. In addition, the positively charged cluster located beneath the B'-helix is suggested as possible NADH binding site in P450nor, from which the direct two-electron transfer to the heme site allows to generate the characteristic intermediate in the NO reduction. These structural characteristics were not observed in structures of monooxygenase P450s, implying that these are factors determining the unique NO reduction activity of P450nor.
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(as it appears on PubMed at http://www.pubmed.gov), where 11051564 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11051564}}
==About this Structure==
==About this Structure==
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[[Category: Cytochrome p450nor]]
[[Category: Cytochrome p450nor]]
[[Category: Nitric oxide reductase]]
[[Category: Nitric oxide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:06:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:42:22 2008''

Revision as of 21:42, 30 June 2008

Image:1ehf.png

Template:STRUCTURE 1ehf

CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S

Template:ABSTRACT PUBMED 11051564

About this Structure

1EHF is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

Reference

Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s., Shimizu H, Park S, Lee D, Shoun H, Shiro Y, J Inorg Biochem. 2000 Aug 31;81(3):191-205. PMID:11051564

Page seeded by OCA on Tue Jul 1 00:42:22 2008

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