1pre

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pre OCA], [http://www.ebi.ac.uk/pdbsum/1pre PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pre RCSB]</span>
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'''PROAEROLYSIN'''
'''PROAEROLYSIN'''
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[[Category: Tsernoglou, D.]]
[[Category: Tsernoglou, D.]]
[[Category: Tucker, A D.]]
[[Category: Tucker, A D.]]
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[[Category: signal]]
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[[Category: Signal]]
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[[Category: toxin (hemolytic polypeptide)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:24:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:31 2008''
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Revision as of 02:24, 3 May 2008

Image:1pre.gif

Template:STRUCTURE 1pre

PROAEROLYSIN


Overview

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

1PRE is a Single protein structure of sequence from Aeromonas hydrophila. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 05:24:09 2008

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