2bf4

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{{Seed}}
 
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[[Image:2bf4.png|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_2bf4", creates the "Structure Box" on the page.
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<StructureSection load='2bf4' size='340' side='right'caption='[[2bf4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bf4]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2bf4| PDB=2bf4 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf4 OCA], [https://pdbe.org/2bf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf4 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NCPR_YEAST NCPR_YEAST] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.<ref>PMID:1730736</ref> <ref>PMID:9368374</ref> <ref>PMID:9468503</ref> <ref>PMID:11485306</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bf4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bf4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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).
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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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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<ref>PMID:16407065</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bf4" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16407065}}, adds the Publication Abstract to the page
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*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16407065 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16407065}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2BF4 is a 2 chains structure of sequences 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].
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==Reference==
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<ref group="xtra">PMID:16407065</ref><references group="xtra"/>
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[[Category: NADPH--hemoprotein reductase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Kelly, S L.]]
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[[Category: Kelly SL]]
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[[Category: Kim, Y.]]
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[[Category: Kim Y]]
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[[Category: Lamb, D C.]]
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[[Category: Lamb DC]]
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[[Category: Lepesheva, G I.]]
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[[Category: Lepesheva GI]]
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[[Category: Podust, L M.]]
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[[Category: Podust LM]]
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[[Category: Waterman, M R.]]
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[[Category: Waterman MR]]
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[[Category: Yermalitskaya, L V.]]
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[[Category: Yermalitskaya LV]]
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[[Category: Yermalitsky, V N.]]
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[[Category: Yermalitsky VN]]
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[[Category: Fad,fmn,nadp,electron transfer]]
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[[Category: Nadph-cytochrome p450 reductase,cpr,diflavin reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:14:53 2009''
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Current revision

A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases.

PDB ID 2bf4

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