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

doi:10.1107/S1744309110012182

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

医学部・微生物学

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

5 被引用数 (Scopus)

抄録

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.

本文言語	英語
ページ（範囲）	608-610
ページ数	3
ジャーナル	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
巻	66
号	5
DOI	https://doi.org/10.1107/S1744309110012182
出版ステータス	出版済み - 29-04-2010

All Science Journal Classification (ASJC) codes

生物理学
構造生物学
生化学
遺伝学
凝縮系物理学

文献へのアクセス

10.1107/S1744309110012182

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引用スタイル

Nuemket, N., Tanaka, Y., Tsukamoto, K., Tsuji, T., Nakamura, K., Kozaki, S., Yao, M., & Tanaka, I. (2010). Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(5), 608-610. https://doi.org/10.1107/S1744309110012182

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

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 {\AA} resolution, respectively. The crystals belonged to space group P212121.",

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

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Nuemket, N, Tanaka, Y, Tsukamoto, K, Tsuji, T, Nakamura, K, Kozaki, S, Yao, M & Tanaka, I 2010, 'Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 66, no. 5, pp. 608-610. https://doi.org/10.1107/S1744309110012182

Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum. / Nuemket, Nipawan; Tanaka, Yoshikazu; Tsukamoto, Kentaro その他.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 5, 29.04.2010, p. 608-610.

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

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AU - Nuemket, Nipawan

AU - Tanaka, Yoshikazu

AU - Tsukamoto, Kentaro

AU - Tsuji, Takao

AU - Nakamura, Keiji

AU - Kozaki, Shunji

AU - Yao, Min

AU - Tanaka, Isao

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AB - 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.

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