Preliminary crystallographic analysis of two oligomerization-deficient mutants of the aerolysin toxin, H132D and H132N, in their proteolyzed forms

被引:3
作者
Pernot, Lucile [1 ]
Schiltz, Marc [2 ]
van der Goot, F. Gisou [1 ]
机构
[1] Ecole Polytech Fed Lausanne, Global Hlth Inst, Fac Life Sci, CH-1015 Lausanne, Switzerland
[2] Ecole Polytech Fed Lausanne, Lab Cristallog, CH-1015 Lausanne, Switzerland
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金
瑞士国家科学基金会;
关键词
aerolysin; virulence factors; Aeromonas hydrophila; SITE-DIRECTED MUTAGENESIS; ACTIVATION; BINDING; COMPLEX; CRYSTALLIZATION; PROAEROLYSIN; DIFFRACTION; HISTIDINES; RECEPTOR; DOMAIN;
D O I
10.1107/S1744309110041035
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Aerolysin is a major virulence factor produced by the Gram-negative bacterium Aeromonas hydrophila and is a member of the beta-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 A 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.
引用
收藏
页码:1626 / 1630
页数:5
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