View source for 9ccq


==Cryo-EM structure of the prepore-like EaCDCL short oligomer==
<StructureSection load='9ccq' size='340' side='right'caption='[[9ccq]], [[Resolution|resolution]] 3.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ccq]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_anophelis_Ag1 Elizabethkingia anophelis Ag1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CCQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.13&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=9ccq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ccq OCA], [https://pdbe.org/9ccq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ccq RCSB], [https://www.ebi.ac.uk/pdbsum/9ccq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ccq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A7T7HCZ8_9FLAO A0A7T7HCZ8_9FLAO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pore-forming proteins comprise a highly diverse group of proteins exemplified by the membrane attack complex/perforin (MACPF), cholesterol-dependent cytolysin (CDC), and gasdermin superfamilies, which all form gigantic pores (&gt;150 angstroms). A recently found family of pore-forming toxins, called CDC-like proteins (CDCLs), are wide-spread in gut microbes and are a prevalent means of antibacterial antagonism. However, the structural aspects of how CDCLs assemble a pore remain a mystery. Here, we report the crystal structure of a proteolytically activated CDCL and cryo-electron microscopy structures of a prepore-like intermediate and a transmembrane pore providing detailed snapshots across the entire pore-forming pathway. These studies reveal a sophisticated array of regulatory features to ensure productive pore formation, and, thus, CDCLs straddle the MACPF, CDC, and gasdermin lineages of the giant pore superfamilies.

Structural basis for the pore-forming activity of a complement-like toxin.,Johnstone BA, Christie MP, Joseph R, Morton CJ, Brown HG, Hanssen E, Sanford TC, Abrahamsen HL, Tweten RK, Parker MW Sci Adv. 2025 Mar 28;11(13):eadt2127. doi: 10.1126/sciadv.adt2127. Epub 2025 Mar , 28. PMID:40153490<ref>PMID:40153490</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ccq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Elizabethkingia anophelis Ag1]]
[[Category: Large Structures]]
[[Category: Brown HG]]
[[Category: Christie MP]]
[[Category: Hanssen E]]
[[Category: Johnstone BA]]
[[Category: Morton CM]]
[[Category: Parker MW]]