2bf4

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[[Image:2bf4.gif|left|200px]]<br /><applet load="2bf4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bf4.gif|left|200px]]
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caption="2bf4, resolution 3.00&Aring;" />
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'''A SECOND FMN-BINDING SITE IN YEAST NADPH-CYTOCHROME P450 REDUCTASE SUGGESTS A NOVEL MECHANISM OF ELECTRON TRANSFER BY DIFLAVIN REDUCTASES.'''<br />
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{{Structure
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|PDB= 2bf4 |SIZE=350|CAPTION= <scene name='initialview01'>2bf4</scene>, resolution 3.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NADPH--hemoprotein_reductase NADPH--hemoprotein reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.4 1.6.2.4]
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|GENE=
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}}
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'''A SECOND FMN-BINDING SITE IN YEAST NADPH-CYTOCHROME P450 REDUCTASE SUGGESTS A NOVEL MECHANISM OF ELECTRON TRANSFER BY DIFLAVIN REDUCTASES.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADPH--hemoprotein_reductase NADPH--hemoprotein reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.4 1.6.2.4] Known structural/functional Site: <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF4 OCA].
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2BF4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF4 OCA].
==Reference==
==Reference==
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A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases., Lamb DC, Kim Y, Yermalitskaya LV, Yermalitsky VN, Lepesheva GI, Kelly SL, Waterman MR, Podust LM, Structure. 2006 Jan;14(1):51-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16407065 16407065]
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A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases., Lamb DC, Kim Y, Yermalitskaya LV, Yermalitsky VN, Lepesheva GI, Kelly SL, Waterman MR, Podust LM, Structure. 2006 Jan;14(1):51-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16407065 16407065]
[[Category: NADPH--hemoprotein reductase]]
[[Category: NADPH--hemoprotein reductase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: nadph-cytochrome p450 reductase]]
[[Category: nadph-cytochrome p450 reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:09 2008''

Revision as of 14:01, 20 March 2008

Image:2bf4.gif


PDB ID 2bf4

Drag the structure with the mouse to rotate
, resolution 3.00Å
Sites:
Ligands: , , and
Activity: NADPH--hemoprotein reductase, with EC number 1.6.2.4
Coordinates: save as pdb, mmCIF, xml



A SECOND FMN-BINDING SITE IN YEAST NADPH-CYTOCHROME P450 REDUCTASE SUGGESTS A NOVEL MECHANISM OF ELECTRON TRANSFER BY DIFLAVIN REDUCTASES.


Overview

NADPH-cytochrome P450 reductase transfers two reducing equivalents derived from a hydride ion of NADPH via FAD and FMN to the large family of microsomal cytochrome P450 monooxygenases in one-electron transfer steps. The mechanism of electron transfer by diflavin reductases remains elusive and controversial. Here, we determined the crystal structure of truncated yeast NADPH-cytochrome P450 reductase, which is functionally active toward its physiological substrate cytochrome P450, and discovered a second FMN binding site at the interface of the connecting and FMN binding domains. The two FMN binding sites have different accessibilities to the bulk solvent and different amino acid environments, suggesting stabilization of different electronic structures of the reduced flavin. Since only one FMN cofactor is required for function, a hypothetical mechanism of electron transfer is discussed that proposes shuttling of a single FMN between these two sites coupled with the transition between two semiquinone forms, neutral (blue) and anionic (red).

About this Structure

2BF4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases., Lamb DC, Kim Y, Yermalitskaya LV, Yermalitsky VN, Lepesheva GI, Kelly SL, Waterman MR, Podust LM, Structure. 2006 Jan;14(1):51-61. PMID:16407065

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