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1pre
From Proteopedia
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==PROAEROLYSIN== | ==PROAEROLYSIN== | ||
| - | <StructureSection load='1pre' size='340' side='right' caption='[[1pre]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='1pre' size='340' side='right'caption='[[1pre]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pre]] is a 2 chain structure with sequence from [ | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1pre_consurf.spt"</scriptWhenChecked> | + | <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/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</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]. | </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="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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pre" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aerolysin|Aerolysin]] | *[[Aerolysin|Aerolysin]] | ||
| - | + | *[[Aerolysin 3D structures|Aerolysin 3D structures]] | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aeromonas | + | [[Category: Aeromonas hydrophila]] |
| - | [[Category: Buckley | + | [[Category: Large Structures]] |
| - | [[Category: Parker | + | [[Category: Buckley JT]] |
| - | [[Category: Postma | + | [[Category: Parker MW]] |
| - | [[Category: Tsernoglou | + | [[Category: Postma JPM]] |
| - | [[Category: Tucker | + | [[Category: Tsernoglou D]] |
| + | [[Category: Tucker AD]] | ||
Current revision
PROAEROLYSIN
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