3c0n
From Proteopedia
(New page: 200px<br /><applet load="3c0n" size="350" color="white" frame="true" align="right" spinBox="true" caption="3c0n, resolution 2.20Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Aerolysin is chiefly responsible for the pathogenicity of Aeromonas | + | 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== | ==About this Structure== | ||
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[[Category: Aeromonas hydrophila]] | [[Category: Aeromonas hydrophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burr, S | + | [[Category: Burr, S E.]] |
| - | [[Category: Goot, G | + | [[Category: Goot, G van der.]] |
[[Category: Pernot, L.]] | [[Category: Pernot, L.]] | ||
[[Category: Schiltz, M.]] | [[Category: Schiltz, M.]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:03 2008'' |
Revision as of 17:08, 21 February 2008
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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 Feb 21 19:08:03 2008
