Ancient weapons: the three-dimensional structure of amoebapore A.
The recently solved three-dimensional structure of amoebapore A, the major pore-forming protein of Entamoeba histolytica, represents the first tertiary structure determined from a parasitic toxin. The implications derived from this solved structure, together with biochemical data, paint a picture of a unique activation mechanism and reveal that a histidine-mediated dimerization of the protein acts as the molecular switch for the formation of oligomeric pores in target cell membranes.
Leippe
Matthias
M
Zoological Institute of the University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany. mleippe@zoologie.uni-kiel.de
Bruhn
Heike
H
Hecht
Oliver
O
Grötzinger
Joachim
J
D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D004748:Entamoeba histolytica / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry*
D007473:Ion Channels; D015800:Protozoan Proteins; C041670:amoebapore proteins, protozoan; D006639:Histidine