4KYP

Beta-Scorpion Toxin folded in the periplasm of E.coli

4KYP の概要

• エントリーDOI: 10.2210/pdb4kyp/pdb
• 関連するPDBエントリー: 1BCG
• 分子名称: Beta-insect excitatory toxin Bj-xtrIT, TRIETHYLENE GLYCOL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: alpha-beta, venom, voltage gated na-channels, toxin
• 由来する生物種: Hottentotta judaicus (Scorpion)
• 細胞内の位置: Secreted: P56637
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38253.16

構造登録者

O'Reilly, A.O.,Cole, A.R.,Lopes, J.L.,Lampert, A.,Wallace, B.A. (登録日: 2013-05-29, 公開日: 2014-02-12, 最終更新日: 2018-01-24)

主引用文献

O'Reilly, A.O.,Cole, A.R.,Lopes, J.L.,Lampert, A.,Wallace, B.A.
Chaperone-mediated native folding of a beta-scorpion toxin in the periplasm of Escherichia coli.
Biochim.Biophys.Acta, 1840:10-15, 2014

PubMed Abstract: Animal neurotoxin peptides are valuable probes for investigating ion channel structure/function relationships and represent lead compounds for novel therapeutics and insecticides. However, misfolding and aggregation are common outcomes when toxins containing multiple disulfides are expressed in bacteria.

PubMed: 23999087
DOI: 10.1016/j.bbagen.2013.08.021

実験手法

X-RAY DIFFRACTION (1.7 Å)