View source for 4kku


==Structure of BesA (Selenomethinone derivative - P212121)==
<StructureSection load='4kku' size='340' side='right'caption='[[4kku]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kku]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKU 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kku OCA], [https://pdbe.org/4kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kku RCSB], [https://www.ebi.ac.uk/pdbsum/4kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kku ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O51166_BORBU O51166_BORBU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35A resolution crystal structure of the BesA adaptor from the spirochete Borrelia burgdorferi solved using selenomethionine derivatized protein. BesA shows the archetypal linear, flexible, multi-domain architecture evident among proteobacteria and retains the lipoyl, beta-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the alpha-hairpin domain shown to establish extensive coiled-coil interactions with the periplasmic entrance helices of the outer membrane-anchored TolC exit duct. This has implications for the modelling of assembled tripartite efflux pumps.

Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi.,Greene NP, Hinchliffe P, Crow A, Ababou A, Hughes C, Koronakis V FEBS Lett. 2013 Jul 9. pii: S0014-5793(13)00520-6. doi:, 10.1016/j.febslet.2013.06.056. PMID:23851070<ref>PMID:23851070</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kku" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi B31]]
[[Category: Large Structures]]
[[Category: Ababou A]]
[[Category: Crow A]]
[[Category: Greene NP]]
[[Category: Hinchliffe P]]
[[Category: Hughes C]]
[[Category: Koronakis V]]