Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum

Nipawan Nuemket, Yoshikazu Tanaka, Kentaro Tsukamoto, Takao Tsuji, Keiji Nakamura, Shunji Kozaki, Min Yao, Isao Tanaka

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Botulinum toxin (BoNT) from Clostridium botulinum OFD05, isolated from bovine botulism, is a D/C mosaic-type BoNT. BoNTs possess binding, translocation and catalytic domains. The BoNT/OFD05 binding domain exhibits significant sequence identity to BoNT/C, which requires a single ganglioside as a binding receptor on neuronal cells, while BoNT/A and BoNT/B require two receptors for specific binding. To determine the binding mechanism of BoNT/OFD05 and its ganglioside receptors on neuronal cells, recombinant BoNT/OFD05 receptor-binding domain has been expressed, purified and crystallized. Native and SeMet-derivative crystals showed X-ray diffraction to 2.8 and 3.1 Å resolution, respectively. The crystals belonged to space group P212121.

Original languageEnglish
Pages (from-to)608-610
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number5
DOIs
Publication statusPublished - 2010 Apr 29
Externally publishedYes

Keywords

  • Botulinum toxins
  • Clostridium botulinum strain OFD05
  • D/C mosaic-type BoNT
  • Receptor-binding domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum'. Together they form a unique fingerprint.

Cite this