View source for 7our


==Wilavidin apo form (P1 form)==
<StructureSection load='7our' size='340' side='right'caption='[[7our]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7our]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gammaproteobacteria_bacterium Gammaproteobacteria bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OUR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7our FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7our OCA], [https://pdbe.org/7our PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7our RCSB], [https://www.ebi.ac.uk/pdbsum/7our PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7our ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3A4VWA2_9GAMM A0A3A4VWA2_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nature's optimization of protein functions is a highly intricate evolutionary process. In addition to optimal tertiary folding, the intramolecular recognition among the monomers that generate higher-order quaternary arrangements is driven by stabilizing interactions that have a pivotal role for ideal activity. Homotetrameric avidin and streptavidin are regularly utilized in many applications, whereby their ultra-high affinity toward biotin is dependent on their quaternary arrangements. In recent years, a new subfamily of avidins was discovered that comprises homodimers rather than tetramers, in which the high affinity toward biotin is maintained. Intriguingly, several of the respective dimers have been shown to assemble into higher-order cylindrical hexamers or octamers that dissociate into dimers upon biotin binding. Here, we present wilavidin, a newly discovered member of the dimeric subfamily, forming hexamers in the apo form, which are uniquely maintained upon biotin binding with six high-affinity binding sites. Removal of the short C-terminal segment of wilavidin resulted in the presence of the dimer only, thus emphasizing the role of this segment in stabilizing the hexamer. Utilization of a hexavalent biotin-binding form of avidin would be beneficial for expanding the biotechnological toolbox. Additionally, this unique family of dimeric avidins and their propensity to oligomerize to hexamers or octamers can serve as a basis for protein oligomerization and intermonomeric recognition as well as cumulative interactions that determine molecular assemblies.

Wilavidin* - a novel member of the avidin family that forms unique biotin-binding hexamers.,Avraham O, Bayer EA, Livnah O FEBS J. 2021 Nov 2. doi: 10.1111/febs.16259. PMID:34726340<ref>PMID:34726340</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7our" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gammaproteobacteria bacterium]]
[[Category: Large Structures]]
[[Category: Avraham O]]
[[Category: Livnah O]]