1pre
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(New page: 200px<br /><applet load="1pre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pre, resolution 2.8Å" /> '''PROAEROLYSIN'''<br />...)
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Revision as of 21:56, 20 November 2007
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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
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