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1t0i

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[[Image:1t0i.jpg|left|200px]]
 
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{{Structure
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==YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase==
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|PDB= 1t0i |SIZE=350|CAPTION= <scene name='initialview01'>1t0i</scene>, resolution 2.00&Aring;
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<StructureSection load='1t0i' size='340' side='right'caption='[[1t0i]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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<table><tr><td colspan='2'>[[1t0i]] 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=1T0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0I FirstGlance]. <br>
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|ACTIVITY=
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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]] 2&#8491;</td></tr>
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|GENE= YLR011w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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|DOMAIN=
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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=1t0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0i OCA], [https://pdbe.org/1t0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0i RCSB], [https://www.ebi.ac.uk/pdbsum/1t0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0i ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1nni|1NNI]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0i OCA], [http://www.ebi.ac.uk/pdbsum/1t0i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0i RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LOT6_YEAST LOT6_YEAST] Has several reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation.<ref>PMID:15184374</ref>
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== Evolutionary Conservation ==
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'''YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0i_consurf.spt"</scriptWhenChecked>
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Flavodoxins are involved in a variety of electron transfer reactions that are essential for life. Although FMN-binding proteins are well characterized in prokaryotic organisms, information is scarce for eukaryotic flavodoxins. We describe the 2.0-A resolution crystal structure of the Saccharomyces cerevisiae YLR011w gene product, a predicted flavoprotein. YLR011wp indeed adopts a flavodoxin fold, binds the FMN cofactor, and self-associates as a homodimer. Despite the absence of the flavodoxin key fingerprint motif involved in FMN binding, YLR011wp binds this cofactor in a manner very analogous to classical flavodoxins. YLR011wp closest structural homologue is the homodimeric Bacillus subtilis Yhda protein (25% sequence identity) whose homodimer perfectly superimposes onto the YLR011wp one. Yhda, whose function is not documented, has 53% sequence identity with the Bacillus sp. OY1-2 azoreductase. We show that YLR011wp has an NAD(P)H-dependent FMN reductase and a strong ferricyanide reductase activity. We further demonstrate a weak but specific reductive activity on azo dyes and nitrocompounds.
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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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==About this Structure==
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</jmolCheckbox>
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1T0I 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=1T0I OCA].
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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=1t0i ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities., Liger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J, van Tilbeurgh H, J Biol Chem. 2004 Aug 13;279(33):34890-7. Epub 2004 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15184374 15184374]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Blondeau K]]
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[[Category: Blondeau, K.]]
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[[Category: Graille M]]
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[[Category: Graille, M.]]
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[[Category: Janin J]]
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[[Category: Janin, J.]]
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[[Category: Leulliot N]]
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[[Category: Leulliot, N.]]
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[[Category: Liger D]]
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[[Category: Liger, D.]]
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[[Category: Quevillon-Cheruel S]]
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[[Category: Quevillon-Cheruel, S.]]
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[[Category: Zhou C-Z]]
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[[Category: Tilbeurgh, H van.]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Zhou, C Z.]]
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[[Category: azoreductase]]
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[[Category: flavodoxin]]
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[[Category: fmn binding protein]]
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[[Category: saccharomyces cerevisiae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:30 2008''
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Current revision

YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase

PDB ID 1t0i

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