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New page: left|200px<br /><applet load="1wlk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wlk, resolution 1.90Å" /> '''L122E mutant of FMN-...
 
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[[Image:1wlk.gif|left|200px]]<br /><applet load="1wlk" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wlk, resolution 1.90&Aring;" />
'''L122E mutant of FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)'''<br />


==About this Structure==
==L122E mutant of FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)==
1WLK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WLK OCA].  
<StructureSection load='1wlk' size='340' side='right'caption='[[1wlk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
[[Category: Desulfovibrio vulgaris]]
== Structural highlights ==
[[Category: Single protein]]
<table><tr><td colspan='2'>[[1wlk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._'Miyazaki_F' Desulfovibrio vulgaris str. 'Miyazaki F']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLK FirstGlance]. <br>
[[Category: Higuchi, Y.]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
[[Category: Shibata, N.]]
<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>
[[Category: FMN]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlk OCA], [https://pdbe.org/1wlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wlk RCSB], [https://www.ebi.ac.uk/pdbsum/1wlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wlk ProSAT]</span></td></tr>
[[Category: electron transport]]
</table>
[[Category: flavoprotein]]
== Function ==
[[Category: fmn]]
[https://www.uniprot.org/uniprot/FMNB_DESVM FMNB_DESVM] Functions as a redox protein with a potential of -325 mV.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wl/1wlk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wlk ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutants of flavin mononucleotide-binding protein (FMN-bp) were made by site-directed mutagenesis to investigate the role of carboxyl-terminal Leu122 of the pairing subunit in controlling redox potentials, binding the prosthetic group, and forming the tertiary and quaternary structure. We compared the oxidation-reduction potentials, FMN-binding properties, and higher structures of wild-type FMN-bp and four mutant proteins (L122Y, L122E, L122K and L122-deleted). We found that the redox potentials were affected by mutations. Also, the affinities of L122E, L122K and L122 deletion mutant apoproteins for FMN were lower than for the wild-type apoprotein, whereas the affinity of L122Y for FMN was increased. Analytical ultracentrifugation showed that the dissociation constants for dimerization of L122E and L122K were larger than for wild-type FMN-bp, whereas the dissociation constants for L122Y and the deletion mutant were lower than for the wild type. Finally, we determined the higher structures of L122Y, L122E and L122K mutants by X-ray crystallography. Our results show that the mutation of Leu122 in FMN-bp changes midpoint potentials, dissociation constants for FMN, and dimer formation, indicating that this residue is important in the pairing subunit.


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:30:45 2007''
Determination of the role of the Carboxyl-terminal leucine-122 in FMN-binding protein by mutational and structural analysis.,Kitamura M, Terakawa K, Inoue H, Hayashida T, Suto K, Morimoto Y, Yasuoka N, Shibata N, Higuchi Y J Biochem. 2007 Apr;141(4):459-68. Epub 2007 Jan 29. PMID:17261542<ref>PMID:17261542</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wlk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio vulgaris str. 'Miyazaki F']]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Shibata N]]
Retrieved from "https://proteopedia.org/1wlk"