3WIN

Clostridium botulinum Hemagglutinin

3WIN の概要

• エントリーDOI: 10.2210/pdb3win/pdb
• 分子名称: HA3, 17 kD hemagglutinin component, HA1, ... (5 entities in total)
• 機能のキーワード: bacterial pathogenesis, bacterial toxins, carbohydrate-binding protein, e-cadherin, epithelial cell, protein complexes, botulinum toxin, hemagglutinin, beta-trefoil, toxin
• 由来する生物種: Clostridium botulinum B; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 162423.77

構造登録者

Amatsu, S.,Sugawara, Y.,Matsumura, T.,Fujinaga, Y.,Kitadokoro, K. (登録日: 2013-09-19, 公開日: 2013-11-06, 最終更新日: 2023-11-08)

主引用文献

Amatsu, S.,Sugawara, Y.,Matsumura, T.,Kitadokoro, K.,Fujinaga, Y.
Crystal Structure of Clostridium botulinum Whole Hemagglutinin Reveals a Huge Triskelion-shaped Molecular Complex
J.Biol.Chem., 288:35617-35625, 2013

PubMed Abstract: Clostridium botulinum HA is a component of the large botulinum neurotoxin complex and is critical for its oral toxicity. HA plays multiple roles in toxin penetration in the gastrointestinal tract, including protection from the digestive environment, binding to the intestinal mucosal surface, and disruption of the epithelial barrier. At least two properties of HA contribute to these roles: the sugar-binding activity and the barrier-disrupting activity that depends on E-cadherin binding of HA. HA consists of three different proteins, HA1, HA2, and HA3, whose structures have been partially solved and are made up mainly of β-strands. Here, we demonstrate structural and functional reconstitution of whole HA and present the complete structure of HA of serotype B determined by x-ray crystallography at 3.5 Å resolution. This structure reveals whole HA to be a huge triskelion-shaped molecule. Our results suggest that whole HA is functionally and structurally separable into two parts: HA1, involved in recognition of cell-surface carbohydrates, and HA2-HA3, involved in paracellular barrier disruption by E-cadherin binding.

PubMed: 24165130
DOI: 10.1074/jbc.M113.521179

実験手法

X-RAY DIFFRACTION (3.5 Å)