Aerolysin--a paradigm for membrane insertion of beta-sheet protein toxins?
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.
Rossjohn
J
J
Ian Potter Foundation Protein Crystallography Laboratory, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Feil
S C
SC
McKinstry
W J
WJ
Tsernoglou
D
D
van der Goot
G
G
Buckley
J T
JT
Parker
M W
MW
D000595:Amino Acid Sequence; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D002463:Cell Membrane Permeability / Q000187:drug effects*; D018360:Crystallography, X-Ray; D003603:Cytotoxins / Q000737:chemistry; D019281:Dimerization; D006460:Hemolysin Proteins / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D011108:Polymers; D052899:Pore Forming Cytotoxic Proteins; D011485:Protein Binding; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D001427:Bacterial Toxins; D003603:Cytotoxins; D006460:Hemolysin Proteins; D007473:Ion Channels; D010940:Plant Proteins; D011108:Polymers; D052899:Pore Forming Cytotoxic Proteins; D011498:Protein Precursors; C064270:hemolytic toxin, Clostridium septicum; C073270:enterolobin protein, Enterolobium contortisiliquum; C032676:aerolysin