3BTA

CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A

3BTA の概要

• エントリーDOI: 10.2210/pdb3bta/pdb
• 分子名称: PROTEIN (BOTULINUM NEUROTOXIN TYPE A), ZINC ION (2 entities in total)
• 機能のキーワード: neurotoxin, zinc protease, sugar binding protein, translocation, toxin
• 由来する生物種: Clostridium botulinum
• 細胞内の位置: Botulinum neurotoxin A light chain: Secreted. Botulinum neurotoxin A heavy chain: Secreted: P10845
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 149545.22

構造登録者

Stevens, R.C.,Lacy, D.B. (登録日: 1998-08-12, 公開日: 1999-10-01, 最終更新日: 2024-10-30)

主引用文献

Lacy, D.B.,Tepp, W.,Cohen, A.C.,DasGupta, B.R.,Stevens, R.C.
Crystal structure of botulinum neurotoxin type A and implications for toxicity.
Nat.Struct.Biol., 5:898-902, 1998

PubMed Abstract: Botulinum neurotoxin type A (BoNT/A) is the potent disease agent in botulism, a potential biological weapon and an effective therapeutic drug for involuntary muscle disorders. The crystal structure of the entire 1,285 amino acid di-chain neurotoxin was determined at 3.3 A resolution. The structure reveals that the translocation domain contains a central pair of alpha-helices 105 A long and a approximately 50 residue loop or belt that wraps around the catalytic domain. This belt partially occludes a large channel leading to a buried, negative active site--a feature that calls for radically different inhibitor design strategies from those currently used. The fold of the translocation domain suggests a mechanism of pore formation different from other toxins. Lastly, the toxin appears as a hybrid of varied structural motifs and suggests a modular assembly of functional subunits to yield pathogenesis.

PubMed: 9783750
DOI: 10.1038/2338

実験手法

X-RAY DIFFRACTION (3.2 Å)