1Z0H

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B

1Z0H の概要

• エントリーDOI: 10.2210/pdb1z0h/pdb
• 関連するPDBエントリー: 1ERW
• 分子名称: Botulinum neurotoxin type B (2 entities in total)
• 機能のキーワード: clostridium botulinum, binding domain, gangliosides, 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: 2
• 化学式量合計: 105460.65

構造登録者

Jayaraman, S.,Eswarmoorthy, S.,Ashraf, S.A.,Smith, L.A.,Swaminathan, S. (登録日: 2005-03-01, 公開日: 2005-03-15, 最終更新日: 2023-08-23)

主引用文献

Jayaraman, S.,Eswaramoorthy, S.,Ahmed, S.A.,Smith, L.A.,Swaminathan, S.
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B.
Biochem.Biophys.Res.Commun., 330:97-103, 2005

PubMed Abstract: Botulinum neurotoxins comprise seven distinct serotypes (A-G) produced by Clostridium botulinum. The crystal structure of the binding domain of the botulinum neurotoxin type B (BBHc) has been determined to 2A resolution. The overall structure of BBHc is well ordered and similar to that of the binding domain of the holotoxin. However, significant structural changes occur at what would be the interface of translocation and binding domains of the holotoxin. The loop 911-924 shows a maximum displacement of 14.8A at the farthest point. The N-terminal helix reorients and moves by 19.5A from its original position. BBHc is compared with the binding domain of the holotoxin of botulinum type A and B, and the tetanus C-fragment to characterize the heavy chain-carbohydrate interactions. The probable reasons for different binding affinity of botulinum and tetanus toxins are discussed.

PubMed: 15781237
DOI: 10.1016/j.bbrc.2005.02.123

実験手法

X-RAY DIFFRACTION (2 Å)