View source for 5imy


==Trapped Toxin==
<StructureSection load='5imy' size='340' side='right'caption='[[5imy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5imy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gardnerella_vaginalis Gardnerella vaginalis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IMY 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]] 2.4&#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=5imy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imy OCA], [https://pdbe.org/5imy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5imy RCSB], [https://www.ebi.ac.uk/pdbsum/5imy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5imy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2YGA4_GARVA B2YGA4_GARVA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cholesterol-dependent cytolysins (CDCs) are a family of pore-forming toxins that punch holes in the outer membrane of eukaryotic cells. Cholesterol serves as the receptor, but a subclass of CDCs first binds to human CD59. Here we describe the crystal structures of vaginolysin and intermedilysin complexed to CD59. These studies, together with small-angle X-ray scattering, reveal that CD59 binds to each at different, though overlapping, sites, consistent with molecular dynamics simulations and binding studies. The CDC consensus undecapeptide motif, which for the CD59-responsive CDCs has a proline instead of a tryptophan in the motif, adopts a strikingly different conformation between the structures; our data suggest that the proline acts as a selectivity switch to ensure CD59-dependent CDCs bind their protein receptor first in preference to cholesterol. The structural data suggest a detailed model of how these water-soluble toxins assemble as prepores on the cell surface.

Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.,Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, Parker MW Structure. 2016 Sep 6;24(9):1488-1498. doi: 10.1016/j.str.2016.06.017. Epub 2016 , Aug 4. PMID:27499440<ref>PMID:27499440</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5imy" style="background-color:#fffaf0;"></div>

==See Also==
*[[CD59|CD59]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gardnerella vaginalis]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Lawrence SL]]
[[Category: Morton CJ]]
[[Category: Parker MW]]