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3c0n
From Proteopedia
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | aerA (Aeromonas hydrophila) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 19:02:03 2008
