1pre: Difference between revisions
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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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Revision as of 05:24, 3 May 2008
PROAEROLYSIN
OverviewOverview
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 StructureAbout this Structure
1PRE is a Single protein structure of sequence from Aeromonas hydrophila. Full crystallographic information is available from OCA.
ReferenceReference
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