Open AccessCrystallization and preliminary X‐ray analysis of the vWA domain of human anthrax toxin receptor 1
Author(s) -
Cai Chenguang,
Zhao Ying,
Tong Xiaohang,
Fu Sheng,
Li Yuanyuan,
Wu Yang,
Li Xumei,
Lou Zhiyong
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110043770
Subject(s) - anthrax toxin , bacillus anthracis , pore forming toxin , von willebrand factor , toxin , receptor , microbiology and biotechnology , extracellular , antigen , virulence factor , chemistry , biology , bacteria , virulence , biochemistry , microbial toxins , immunology , platelet , genetics , recombinant dna , fusion protein , gene
The Gram‐positive spore‐forming bacterium Bacillus anthracis causes anthrax by secreting anthrax toxin, which consists of protective antigen (PA), lethal factor and oedema factor. Binding of PA to receptors triggers the multi‐step process of anthrax toxin entry into target cells. Two distinct cellular receptors, ANTXR1 (also known as tumour endothelial marker 8; TEM8) and ANTXR2 (also known as capillary morphogenesis protein 2; CMG2), for anthrax toxin have been identified. Although the crystal structure of the extracellular von Willebrand factor A (vWA) domain of CMG2 has been reported, the difference between the vWA domains of TEM8 and CMG2 remains unclear because there are no structural data for the TEM8 vWA domain. In this report, the TEM8 vWA domain was expressed, purified and crystallized. X‐ray diffraction data were collected to 1.8 Å resolution from a single crystal, which belonged to space group P 1 with unit‐cell parameters a = 65.9, b = 66.1, c = 74.4 Å, α = 63.7, β = 88.2, γ = 59.9°.