8BO0

Solution structure of Lqq4 toxin from Leiurus quinquestriatus quinquestriatus

8BO0 の概要

• エントリーDOI: 10.2210/pdb8bo0/pdb
• NMR情報: BMRB: 34771
• 分子名称: Alpha-toxin Lqq4 (1 entity in total)
• 機能のキーワード: toxin, protein
• 由来する生物種: Leiurus quinquestriatus quinquestriatus (Egyptian scorpion)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7211.23

構造登録者

Mineev, K.S.,Motov, V.V.,Vassilevski, A.A.,Chernykh, M.A.,Kuzmenkov, A.I. (登録日: 2022-11-14, 公開日: 2023-09-20, 最終更新日: 2024-11-20)

主引用文献

Mineev, K.S.,Chernykh, M.A.,Motov, V.V.,Prudnikova, D.A.,Pavlenko, D.M.,Kuzmenkov, A.I.,Peigneur, S.,Tytgat, J.,Vassilevski, A.A.
A scorpion toxin affecting sodium channels shows double cis-trans isomerism.
Febs Lett., 597:2358-2368, 2023

PubMed Abstract: Scorpion α-toxins (α-NaTx) inhibiting the inactivation of voltage-gated sodium channels (Na ) are a well-studied family of small proteins. We previously showed that the structure of α-NaTx specificity module responsible for selective Na binding is governed by an interplay between the nest and niche protein motifs. Here, we report the solution structure of the toxin Lqq4 from the venom of the scorpion Leiurus quinquestriatus. Unexpectedly, we find that this toxin presents an ensemble of long-lived structurally distinct states. We unequivocally assign these states to the alternative configurations (cis-trans isomers) of two peptide bonds: V56-P57 and C17-G18; neither of the cis isomers has been described in α-NaTx so far. We argue that the native conformational space of α-NaTx is wider than assumed previously.

PubMed: 37501371
DOI: 10.1002/1873-3468.14705

実験手法

SOLUTION NMR