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New page: left|200px<br /><applet load="1pre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pre, resolution 2.8Å" /> '''PROAEROLYSIN'''<br />...
 
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[[Image:1pre.gif|left|200px]]<br /><applet load="1pre" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1pre, resolution 2.8&Aring;" />
'''PROAEROLYSIN'''<br />


==Overview==
==PROAEROLYSIN==
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.
<StructureSection load='1pre' size='340' side='right'caption='[[1pre]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pre]] is a 2 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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=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>
</table>
== 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1pre_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pre ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
1PRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7510043 7510043]
</div>
<div class="pdbe-citations 1pre" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aerolysin|Aerolysin]]
*[[Aerolysin 3D structures|Aerolysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeromonas hydrophila]]
[[Category: Aeromonas hydrophila]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Buckley, J.T.]]
[[Category: Buckley JT]]
[[Category: Parker, M.W.]]
[[Category: Parker MW]]
[[Category: Postma, J.P.M.]]
[[Category: Postma JPM]]
[[Category: Tsernoglou, D.]]
[[Category: Tsernoglou D]]
[[Category: Tucker, A.D.]]
[[Category: Tucker AD]]
[[Category: signal]]
[[Category: toxin (hemolytic polypeptide)]]
 
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