1PRE

PROAEROLYSIN

Summary for 1PRE

• Entry DOI: 10.2210/pdb1pre/pdb
• Descriptor: PROAEROLYSIN (2 entities in total)
• Functional Keywords: toxin (hemolytic polypeptide)
• Biological source: Aeromonas hydrophila
• Cellular location: Secreted: P09167
• Total number of polymer chains: 2
• Total formula weight: 103960.91

Authors

Parker, M.W.,Buckley, J.T.,Postma, J.P.M.,Tucker, A.D.,Tsernoglou, D. (deposition date: 1995-09-15, release date: 1996-10-14, Last modification date: 2024-10-16)

Primary citation

Parker, M.W.,Buckley, J.T.,Postma, J.P.,Tucker, A.D.,Leonard, K.,Pattus, F.,Tsernoglou, D.
Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.
Nature, 367:292-295, 1994

PubMed Abstract: 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.

PubMed: 7510043
DOI: 10.1038/367292a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)