3c0n: Difference between revisions
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'''Crystal structure of the proaerolysin mutant Y221G at 2.2 A''' | {{Structure | ||
|PDB= 3c0n |SIZE=350|CAPTION= <scene name='initialview01'>3c0n</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= aerA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 Aeromonas hydrophila]) | |||
}} | |||
'''Crystal structure of the proaerolysin mutant Y221G at 2.2 A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3C0N is a [ | 3C0N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C0N OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7510043 7510043] | ||
[[Category: Aeromonas hydrophila]] | [[Category: Aeromonas hydrophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:02:03 2008'' | ||
Revision as of 17:02, 20 March 2008
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| 3c0n, resolution 2.20Å | |||||||||||||
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| Gene: | aerA (Aeromonas hydrophila) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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