Open AccessPreliminary crystallographic analysis of two oligomerization‐deficient mutants of the aerolysin toxin, H132D and H132N, in their proteolyzed forms
Author(s) -
Pernot Lucile,
Schiltz Marc,
Van Der Goot F. Gisou
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110041035
Subject(s) - aerolysin , mutant , aeromonas hydrophila , toxin , virulence factor , virulence , biology , microbial toxins , microbiology and biotechnology , chemistry , biophysics , bacteria , biochemistry , genetics , gene
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 C 2. 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.