1pre: Difference between revisions

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{{STRUCTURE_1pre|  PDB=1pre  |  SCENE=  }}  
{{STRUCTURE_1pre|  PDB=1pre  |  SCENE=  }}  


'''PROAEROLYSIN'''
===PROAEROLYSIN===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_7510043}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7510043}}


==About this Structure==
==About this Structure==
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[[Category: Tucker, A D.]]
[[Category: Tucker, A D.]]
[[Category: Signal]]
[[Category: Signal]]
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