Abstract
The determination of the crystal structure of the bacterial protein proaerolysin provided the first view of a pore-forming toxin constructed mainly from beta-sheet. The structure that was obtained and subsequent crystallographic and biochemical studies have together allowed us to explain how the toxin is transformed from a water-soluble dimer to a heptameric transmembrane pore. Recent discoveries of structural similarities between aerolysin and other toxins suggest that the structure/function studies we have made may prove useful in understanding the actions of a number of pore-forming proteins.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Amino Acid Sequence
-
Bacterial Toxins / chemistry*
-
Bacterial Toxins / metabolism
-
Bacterial Toxins / pharmacology
-
Cell Membrane Permeability / drug effects*
-
Crystallography, X-Ray
-
Cytotoxins / chemistry
-
Dimerization
-
Hemolysin Proteins / chemistry
-
Ion Channels / chemistry*
-
Models, Molecular*
-
Molecular Sequence Data
-
Plant Proteins / chemistry
-
Polymers
-
Pore Forming Cytotoxic Proteins
-
Protein Binding
-
Protein Conformation
-
Protein Precursors / chemistry
-
Protein Structure, Secondary*
-
Sequence Alignment
-
Sequence Homology, Amino Acid
-
Structure-Activity Relationship
Substances
-
Bacterial Toxins
-
Cytotoxins
-
Hemolysin Proteins
-
Ion Channels
-
Plant Proteins
-
Polymers
-
Pore Forming Cytotoxic Proteins
-
Protein Precursors
-
hemolytic toxin, Clostridium septicum
-
enterolobin protein, Enterolobium contortisiliquum
-
aerolysin