1pre

<table><tr><td colspan='2'>[[1pre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRE FirstGlance]. <br>

</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=1pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pre OCA], [https://pdbe.org/1pre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pre RCSB], [https://www.ebi.ac.uk/pdbsum/1pre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pre ProSAT]</span></td></tr>

[[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 ==

Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels.

Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.,Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043<ref>PMID:7510043</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Aeromonas liquefaciens kluyver and van niel 1936]]

[[Category: Buckley, J T]]

[[Category: Parker, M W]]

[[Category: Postma, J P.M]]

[[Category: Tsernoglou, D]]

[[Category: Tucker, A D]]