1vfr

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[[Image:1vfr.jpg|left|200px]]<br /><applet load="1vfr" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vfr, resolution 1.8&Aring;" />
 
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'''THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI'''<br />
 
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==Overview==
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==THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI==
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We have solved the crystal structure of FRase I, the major NAD(P)H:FMN, oxidoreductase of Vibrio fischeri, by the multiple isomorphous replacement, method (MIR) at 1.8 A resolution with the conventional R factor of 0.187., The crystal structure of FRase I complexed with its competitive inhibitor, dicoumarol, has also been solved at 2.2 A resolution with the conventional, R factor of 0.161. FRase I is a homodimer, having one FMN cofactor per, subunit, which is situated at the interface of two subunits. The overall, fold can be divided into two domains; 80% of the residues form a rigid, core and the remaining, a small flexible domain. The overall core folding, is similar to those of an NADPH-dependent flavin reductase of Vibrio, harveyi (FRP) and the NADH oxidase of Thermus thermophilus (NOX) in spite, of the very low identity in amino acid sequences (10% with FRP and 21%, with NOX). 56% of alpha-carbons of FRase I core residues could be, superposed onto NOX counterparts with an r.m.s. distance of 1.2 A. The, remaining residues have relatively high B-values and may be essential for, defining the substrate specificity. Indeed, one of them, Phe124, was found, to participate in the binding of dicoumarol through stacking to one of the, rings of dicoumarol. Upon binding of dicoumarol, most of the exposed, re-face of the FMN cofactor is buried, which is consistent with the ping, pong bi bi catalytic mechanism.
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<StructureSection load='1vfr' size='340' side='right'caption='[[1vfr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1vfr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VFR FirstGlance]. <br>
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1VFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_fischeri Vibrio fischeri] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_1.5.1.29 Transferred entry: 1.5.1.29], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.8.1 1.6.8.1] Known structural/functional Sites: <scene name='pdbsite=FM2:Cofactor'>FM2</scene> and <scene name='pdbsite=FMN:Cofactor'>FMN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFR OCA].
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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]] 1.8&#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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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==Reference==
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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=1vfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfr OCA], [https://pdbe.org/1vfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vfr RCSB], [https://www.ebi.ac.uk/pdbsum/1vfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vfr ProSAT]</span></td></tr>
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1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins., Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M, J Mol Biol. 1998 Jul 10;280(2):259-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9654450 9654450]
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</table>
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[[Category: Single protein]]
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== Function ==
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[[Category: Transferred entry: 1.5.1.29]]
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[https://www.uniprot.org/uniprot/FRA1_ALIFS FRA1_ALIFS] Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective.
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[[Category: Vibrio fischeri]]
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== Evolutionary Conservation ==
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[[Category: Adman, E.T.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Kobori, T.]]
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Check<jmol>
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[[Category: Koike, H.]]
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<jmolCheckbox>
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[[Category: Murphy, M.E.P.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vf/1vfr_consurf.spt"</scriptWhenChecked>
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[[Category: Saigo, K.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Sasaki, H.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Tanokura, M.]]
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</jmolCheckbox>
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[[Category: Zenno, S.]]
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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=1vfr ConSurf].
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[[Category: FMN]]
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<div style="clear:both"></div>
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[[Category: bioluminescence]]
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__TOC__
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[[Category: fmn]]
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</StructureSection>
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[[Category: nad(p)h]]
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[[Category: Aliivibrio fischeri]]
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[[Category: oxidoreductase]]
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[[Category: Large Structures]]
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[[Category: vibrio fischeri]]
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[[Category: Adman ET]]
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[[Category: Kobori T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:16:59 2008''
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[[Category: Koike H]]
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[[Category: Murphy MEP]]
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[[Category: Saigo K]]
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[[Category: Sasaki H]]
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[[Category: Tanokura M]]
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[[Category: Zenno S]]

Current revision

THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI

PDB ID 1vfr

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