3c0o: Difference between revisions
New page: left|200px<br /><applet load="3c0o" size="350" color="white" frame="true" align="right" spinBox="true" caption="3c0o, resolution 2.50Å" /> '''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 19:08:01 2008'' | ||
Revision as of 17:08, 21 February 2008
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Crystal structure of the proaerolysin mutant Y221G complexed with mannose-6-phosphate
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
3C0O is a Single protein structure of sequence from Aeromonas hydrophila with ACT and M6P as ligands. Known structural/functional Sites: AC1, AC2 and AC3. 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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