1F82

BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN

1F82 の概要

• エントリーDOI: 10.2210/pdb1f82/pdb
• 関連するPDBエントリー: 1F83 3BTA
• 分子名称: BOTULINUM NEUROTOXIN TYPE B, ZINC ION (3 entities in total)
• 機能のキーワード: zinc dependent protease, botulinum neurotoxin, 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: 49076.03

構造登録者

Hanson, M.A.,Stevens, R.C. (登録日: 2000-06-28, 公開日: 2000-08-16, 最終更新日: 2024-02-07)

主引用文献

Hanson, M.A.,Stevens, R.C.
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution.
Nat.Struct.Biol., 7:687-692, 2000

PubMed Abstract: Botulinum neurotoxin serotype B is a zinc protease that disrupts neurotransmitter release by cleaving synaptobrevin-II (Sb2), one of three SNARE proteins involved in neuronal synaptic vesicle fusion. The three-dimensional crystal structure of the apo botulinum neurotoxin serotype B catalytic domain (BoNT/B-LC) has been determined to 2.2 A resolution, and the complex of cleaved Sb2 with the catalytic domain (Sb2-BoNT/B-LC) has been determined to 2.0 A resolution. A comparison of the holotoxin catalytic domain and the isolated BoNT/B-LC structure shows a rearrangement of three active site loops. This rearrangement exposes the BoNT/B active site. The Sb2-BoNT/B-LC structure illustrates two distinct binding regions, which explains the specificity of each botulinum neurotoxin for its synaptic vesicle protein. This observation provides an explanation for the proposed cooperativity between binding of full-length substrate and catalysis and suggest a mechanism of synaptobrevin proteolysis employed by the clostridial neurotoxins.

PubMed: 10932255
DOI: 10.1038/77997

実験手法

X-RAY DIFFRACTION (2.2 Å)