1bu7: Difference between revisions
New page: left|200px<br /><applet load="1bu7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bu7, resolution 1.65Å" /> '''CRYOGENIC STRUCTURE ... |
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[[Image:1bu7.gif|left|200px]]<br /><applet load="1bu7" size=" | [[Image:1bu7.gif|left|200px]]<br /><applet load="1bu7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bu7, resolution 1.65Å" /> | caption="1bu7, resolution 1.65Å" /> | ||
'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN'''<br /> | '''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the complex between the heme- and FMN-binding | The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450. | ||
==About this Structure== | ==About this Structure== | ||
1BU7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http:// | 1BU7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Unspecific monooxygenase]] | [[Category: Unspecific monooxygenase]] | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: Poulos, T | [[Category: Poulos, T L.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: p450]] | [[Category: p450]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:09 2008'' | ||
Revision as of 12:59, 21 February 2008
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CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
OverviewOverview
The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450.
About this StructureAbout this Structure
1BU7 is a Single protein structure of sequence from Bacillus megaterium with and as ligands. Active as Unspecific monooxygenase, with EC number 1.14.14.1 Full crystallographic information is available from OCA.
ReferenceReference
Structure of a cytochrome P450-redox partner electron-transfer complex., Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL, Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1863-8. PMID:10051560
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