1pre: Difference between revisions

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[[Image:1pre.gif|left|200px]]
{{Seed}}
[[Image:1pre.png|left|200px]]


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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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:24:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:10:57 2008''

Revision as of 18:10, 27 July 2008

File:1pre.png

Template:STRUCTURE 1pre

PROAEROLYSIN

Template:ABSTRACT PUBMED 7510043

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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