6THY

Botulinum neurotoxin A3 Hc domain in complex with GD1a

これはPDB形式変換不可エントリーです。

6THY の概要

• エントリーDOI: 10.2210/pdb6thy/pdb
• 関連するPDBエントリー: 2vu9 5tpc 6f0o
• 分子名称: BoNT/A3, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, HEXAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: botulinum, neurotoxin, ganglioside, gd1a, toxin
• 由来する生物種: Clostridium botulinum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52141.10

構造登録者

Gregory, K.S.,Acharya, K.R.,Liu, S.M. (登録日: 2019-11-21, 公開日: 2020-01-29, 最終更新日: 2024-01-24)

主引用文献

Gregory, K.S.,Liu, S.M.,Acharya, K.R.
Crystal structure of botulinum neurotoxin subtype A3 cell binding domain in complex with GD1a co-receptor ganglioside.
Febs Open Bio, 10:298-305, 2020

PubMed Abstract: Botulinum neurotoxins (BoNTs) are one of the most toxic proteins known to humans. Their molecular structure is comprised of three essential domains-a cell binding domain (H ), translocation domain and catalytic domain (light chain) . The H domain facilitates the highly specific binding of BoNTs to the neuronal membrane via a dual-receptor complex involving a protein receptor and a ganglioside. Variation in activity/toxicity across subtypes of serotype A has been attributed to changes in protein and ganglioside interactions, and their implications are important in the design of novel BoNT-based therapeutics. Here, we present the structure of BoNT/A3 cell binding domain (H /A3) in complex with the ganglioside GD1a at 1.75 Å resolution. The structure revealed that six residues interact with the three outermost monosaccharides of GD1a through several key hydrogen bonding interactions. A detailed comparison of structures of H /A3 with H /A1 revealed subtle conformational differences at the ganglioside binding site upon carbohydrate binding.

PubMed: 31945264
DOI: 10.1002/2211-5463.12790

実験手法

X-RAY DIFFRACTION (1.75 Å)