1S0C

Crystal structure of botulinum neurotoxin type B at pH 5.0

1S0C の概要

• エントリーDOI: 10.2210/pdb1s0c/pdb
• 関連するPDBエントリー: 1EPW 1G9A 1S0B 1S0D 1S0E 1S0F 1S0G
• 分子名称: Botulinum neurotoxin type B, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: botulinum, neurotoxin, ph, metals, toxin, hydrolase
• 由来する生物種: Clostridium botulinum
• 細胞内の位置: Botulinum neurotoxin B light chain: Secreted. Botulinum neurotoxin B heavy chain: Secreted: P10844
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 150978.94

構造登録者

Eswaramoorthy, S.,Kumaran, D.,Keller, J.,Swaminathan, S. (登録日: 2003-12-30, 公開日: 2004-03-16, 最終更新日: 2024-11-13)

主引用文献

Eswaramoorthy, S.,Kumaran, D.,Keller, J.,Swaminathan, S.
Role of metals in the biological activity of Clostridium botulinum neurotoxins
Biochemistry, 43:2209-2216, 2004

PubMed Abstract: Clostridium botulinum neurotoxins are the most potent toxins to humans and cause paralysis by blocking neurotransmitter release at the presynaptic nerve terminals. The toxicity involves four steps, viz., binding to neuronal cells, internalization, translocation, and catalytic activity. While the catalytic activity is a zinc endopeptidase activity on the SNARE complex proteins, the translocation is believed to be a pH-dependent process allowing the translocation domain to change its conformation to penetrate the endosomal membrane. Here, we report the crystal structures of botulinum neurotoxin type B at various pHs and of an apo form of the neurotoxin, and discuss the role of metal ions and the effect of pH variation in the biological activity. Except for the perturbation of a few side chains, the conformation of the catalytic domain is unchanged in the zinc-depleted apotoxin, suggesting that zinc's role is catalytic. We have also identified two calcium ions in the molecule and present biochemical evidence to show that they play a role in the translocation of the light chain through the membrane.

PubMed: 14979717
DOI: 10.1021/bi035844k

実験手法

X-RAY DIFFRACTION (2.2 Å)