3c0n: Difference between revisions
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'''Crystal structure of the proaerolysin mutant Y221G at 2.2 A''' | '''Crystal structure of the proaerolysin mutant Y221G at 2.2 A''' | ||
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[[Category: Schiltz, M.]] | [[Category: Schiltz, M.]] | ||
[[Category: Thurnheer, S.]] | [[Category: Thurnheer, S.]] | ||
[[Category: | [[Category: Cytolytic toxin]] | ||
[[Category: | [[Category: Pore-forming toxin]] | ||
[[Category: | [[Category: Toxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:15:53 2008'' | |||
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Revision as of 18:15, 4 May 2008
Crystal structure of the proaerolysin mutant Y221G at 2.2 A
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
3C0N 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 Sun May 4 21:15:53 2008
