This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 15: | Line 15: | ||
[[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]] | ||
| Line 27: | Line 27: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 11:59:38 2008
