1pre

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{{STRUCTURE_1pre| PDB=1pre | SCENE= }}
{{STRUCTURE_1pre| PDB=1pre | SCENE= }}
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'''PROAEROLYSIN'''
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===PROAEROLYSIN===
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==Overview==
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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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{{ABSTRACT_PUBMED_7510043}}
==About this Structure==
==About this Structure==
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[[Category: Tucker, A D.]]
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Revision as of 18:10, 27 July 2008

Image:1pre.png

Template:STRUCTURE 1pre

PROAEROLYSIN

Template:ABSTRACT PUBMED 7510043

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

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