| Literature DB >> 24419620 |
Chikako Iwasa1, Takashi Tonozuka1, Masaya Shinoda1, Yoshimasa Sagane2, Koichi Niwa2, Toshihiro Watanabe2, Hiromi Yoshida3, Shigehiro Kamitori3, Toshifumi Takao4, Keiji Oguma5, Atsushi Nishikawa1.
Abstract
The haemagglutinin (HA) complex of Clostridium botulinum type C toxin is composed of three types of subcomponents: HA33, HA17 and HA70 (also known as HA1, HA2 and HA3, respectively). Here, a 260 kDa HA17-HA70 complex was crystallized. His-tagged HA17 and maltose-binding-protein-tagged HA70 were expressed in Escherichia coli and their complex was affinity-purified using a combination of amylose resin chromatography and nickel-nitrilotriacetic acid agarose chromatography. Diffraction data were collected to 8.0 Å resolution and the crystal belonged to the tetragonal space group P4(1)2(1)2. The molecular-replacement solution indicated that one molecule of HA17 was bound to each HA70 monomer.Entities:
Keywords: Clostridium botulinum; haemagglutinin; lectins; neurotoxins
Mesh:
Substances:
Year: 2013 PMID: 24419620 PMCID: PMC3943108 DOI: 10.1107/S2053230X13032378
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056