1bvy
From Proteopedia
(New page: 200px<br /><applet load="1bvy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvy, resolution 2.03Å" /> '''COMPLEX OF THE HEME ...) |
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| - | [[Image:1bvy.gif|left|200px]]<br /><applet load="1bvy" size=" | + | [[Image:1bvy.gif|left|200px]]<br /><applet load="1bvy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bvy, resolution 2.03Å" /> | caption="1bvy, resolution 2.03Å" /> | ||
'''COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)'''<br /> | '''COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)'''<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== | ||
| - | 1BVY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM, FMN 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:// | + | 1BVY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=FMN:'>FMN</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=1BVY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Unspecific monooxygenase]] | [[Category: Unspecific monooxygenase]] | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
| - | [[Category: Peterson, J | + | [[Category: Peterson, J A.]] |
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
| - | [[Category: Sevrioukova, I | + | [[Category: Sevrioukova, I F.]] |
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: hemoprotein]] | [[Category: hemoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:38 2008'' |
Revision as of 09:59, 21 February 2008
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COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)
Overview
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
1BVY is a Protein complex structure of sequences 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.
Reference
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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