1bu7: Difference between revisions
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[[Image:1bu7.gif|left|200px]] | [[Image:1bu7.gif|left|200px]] | ||
'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN''' | {{Structure | ||
|PDB= 1bu7 |SIZE=350|CAPTION= <scene name='initialview01'>1bu7</scene>, resolution 1.65Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BU7 is a [ | 1BU7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU7 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10051560 10051560] | ||
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: p450]] | [[Category: p450]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:48 2008'' |
Revision as of 11:15, 20 March 2008
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, resolution 1.65Å | |||||||
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Ligands: | and | ||||||
Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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