Preliminary crystallographic analysis of two oligomerization-deficient mutants of the aerolysin toxin, H132D and H132N, in their proteolyzed forms.
Aerolysin is a major virulence factor produced by the Gram-negative bacterium Aeromonas hydrophila and is a member of the β-pore-forming toxin family. Two oligomerization-deficient aerolysin mutants, H132D and H132N, have been overproduced, proteolyzed by trypsin digestion and purified. Crystals were grown from the proteolyzed forms and diffraction data were collected for the two mutants to 2.1 and 2.3 Å resolution, respectively. The prism-shaped crystals belonged to space group C2. The crystal structure of the mutants in the mature, but not heptameric, aerolysin form will provide insight into the intermediate states in the oligomerization process of a pore-forming toxin.
Global Health Institute, Ecole Polytechnique Fédérale de Lausanne, Faculty of Life Sciences, Station 15, CH-1015 Lausanne, Switzerland. lucile.pernot@unige.ch
Lucile
L
Pernot
Marc
M
Schiltz
F Gisou
FG
van der Goot
D016980:Aeromonas hydrophila / Q000737:chemistry*; D001427:Bacterial Toxins / Q000737:chemistry*; D002850:Chromatography, Gel; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D050505:Mutant Proteins / Q000737:chemistry*; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry*; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational
D001427:Bacterial Toxins; D050505:Mutant Proteins; D052899:Pore Forming Cytotoxic Proteins; C032676:aerolysin