Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

被引：16

作者：

Feil, SC

Rossjohn, J

Rohde, K

Tweten, RK

Parker, MW

机构：

[1] ST VINCENTS INST MED RES,IAN POTTER FDN,PROTEIN CRYSTALLOG LAB,FITZROY,VIC 3065,AUSTRALIA

[2] UNIV OKLAHOMA,HLTH SCI CTR,DEPT MICROBIOL & IMMUNOL,OKLAHOMA CITY,OK 73190

来源：

FEBS LETTERS | 1996年 / 397卷 / 2-3期

关键词：

perfringolysin O; thiol-activated cytolysin; pore-forming toxin; crystallization; X-ray diffraction;

D O I：

10.1016/S0014-5793(96)01200-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin O, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C222(1) with cell dimensions of a = 47.8 Angstrom, b = 182.0 Angstrom and c = 175.5 Angstrom and the crystals diffract to beyond 2.5 Angstrom resolution, In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P222(1) with unit cell dimensions a = 47.1 Angstrom, b = 166.1 Angstrom and c = 214.0 Angstrom and with diffraction observed to 2.4 Angstrom resolution.

引用

页码：290 / 292

页数：3

共 16 条

[1] Phospholipase C and perfringolysin O from Clostridium perfringens upregulate endothelial cell-leukocyte adherence molecule 1 and intercellular leukocyte adherence molecule 1 expression and induce interleukin-8 synthesis in cultured human umbilical vein endothelial cells [J].