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1bu7

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[[Image:1bu7.gif|left|200px]]
[[Image:1bu7.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1bu7 |SIZE=350|CAPTION= <scene name='initialview01'>1bu7</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1bu7", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1bu7| PDB=1bu7 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu7 OCA], [http://www.ebi.ac.uk/pdbsum/1bu7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bu7 RCSB]</span>
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}}
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'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN'''
'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN'''
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[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Poulos, T L.]]
[[Category: Poulos, T L.]]
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[[Category: fatty acid monooxygenase]]
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[[Category: Fatty acid monooxygenase]]
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[[Category: hemoprotein]]
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[[Category: Hemoprotein]]
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[[Category: p450]]
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[[Category: P450]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:57:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:19 2008''
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Revision as of 08:57, 2 May 2008

Image:1bu7.gif

Template:STRUCTURE 1bu7

CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN


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

1BU7 is a Single protein structure of sequence from Bacillus megaterium. 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 Fri May 2 11:57:39 2008

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