Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum.
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 A resolution, respectively. The crystals belonged to space group P2(1)2(1)2(1).
Nuemket
Nipawan
N
Graduate School of Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.
Tanaka
Yoshikazu
Y
Tsukamoto
Kentaro
K
Tsuji
Takao
T
Nakamura
Keiji
K
Kozaki
Shunji
S
Yao
Min
M
Tanaka
Isao
I
D001905:Botulinum Toxins / Q000737:chemistry*; D003014:Clostridium botulinum / Q000737:chemistry*; D018360:Crystallography, X-Ray; D009498:Neurotoxins / Q000737:chemistry*; D054730:Protein Interaction Domains and Motifs
D009498:Neurotoxins; C096325:botulinum toxin type D; D001905:Botulinum Toxins; C096324:botulinum toxin type C
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