View source for 5jzt


==Cryo-EM structure of aerolysin pore in LMNG micelle==
<SX load='5jzt' size='340' side='right' viewer='molstar' caption='[[5jzt]], [[Resolution|resolution]] 7.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jzt]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JZT 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]] 7.4&#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=5jzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jzt OCA], [https://pdbe.org/5jzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jzt RCSB], [https://www.ebi.ac.uk/pdbsum/5jzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jzt ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/AERA_AERHY AERA_AERHY] Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis.
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== Publication Abstract from PubMed ==
Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-soluble monomers and subsequently bind the membrane of target cells. Then, they assemble into circular oligomers, which undergo conformational changes that allow membrane insertion leading to pore formation and potentially cell death. Aerolysin, produced by the human pathogen Aeromonas hydrophila, is the founding member of a major PFT family found throughout all kingdoms of life. We report cryo-electron microscopy structures of three conformational intermediates and of the final aerolysin pore, jointly providing insight into the conformational changes that allow pore formation. Moreover, the structures reveal a protein fold consisting of two concentric beta-barrels, tightly kept together by hydrophobic interactions. This fold suggests a basis for the prion-like ultrastability of aerolysin pore and its stoichiometry.

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.,Iacovache I, De Carlo S, Cirauqui N, Dal Peraro M, van der Goot FG, Zuber B Nat Commun. 2016 Jul 13;7:12062. doi: 10.1038/ncomms12062. PMID:27405240<ref>PMID:27405240</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Aerolysin 3D structures|Aerolysin 3D structures]]
== References ==
<references/>
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[[Category: Aeromonas hydrophila]]
[[Category: Large Structures]]
[[Category: Iacovache I]]
[[Category: Zuber B]]