3c0n: Difference between revisions

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==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.

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==

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[[Category: Aeromonas hydrophila]]

[[Category: Single protein]]

[[Category: Burr, S.E.]]

[[Category: Burr, S E.]]

[[Category: Goot, G.van.der.]]

[[Category: Goot, G van der.]]

[[Category: Pernot, L.]]

[[Category: Schiltz, M.]]

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[[Category: toxin]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:03 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Aeromonas hydrophila]]
 [[Category: Single protein]]
-[[Category: Burr, S.E.]]
+[[Category: Burr, S E.]]
-[[Category: Goot, G.van.der.]]
+[[Category: Goot, G van der.]]
 [[Category: Pernot, L.]]
 [[Category: Schiltz, M.]]
@@ Line 22: / Line 22: @@
 [[Category: toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:24:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:03 2008''