2KBJ

solution structure of BmKalphaTx11 (minor conformation)

2KBJ の概要

• エントリーDOI: 10.2210/pdb2kbj/pdb
• 関連するPDBエントリー: 2KBH 2KBK
• 分子名称: Toxin Bmka2 (1 entity in total)
• 機能のキーワード: protein, ionic channel inhibitor, neurotoxin, secreted, sodium channel inhibitor, toxin
• 由来する生物種: Mesobuthus martensii (Manchurian scorpion)
• 細胞内の位置: Secreted: Q9NJC7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7468.42

構造登録者

Zhu, J.,Wu, H. (登録日: 2008-11-28, 公開日: 2009-12-08, 最終更新日: 2024-11-06)

主引用文献

Zhu, J.,Tong, X.,Cao, C.,Wu, G.,Zhang, N.,Wu, H.
Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch
Biochem.Biophys.Res.Commun., 391:627-633, 2010

PubMed Abstract: The solution structure of BmKalphaTx11 presented by this paper is distinctive from any other structures of wide-type scorpion alpha-toxins reported so far, for its trans-9,10 peptide bond conformation is accompanied by 'protruding' topology of the 'NC-domain'. The orientation of the C-tail of BmKalphaTx11 is obviously different from that of classical alpha-toxins (e.g., AaH2, BmK-M8), despite the fact that they share common trans conformation of peptide bond between residues 9 and 10. Accordingly, there must be other structural factors dominating the orientation of the C-tail except the conformation of peptide bond 9-10. Our study reveals that residues at position 58 play an important role in it, and different type of residues at this position (e.g., Lys, Arg, Met, Ile) result in different spatial relationship between the C-terminus and the 'five-residue-turn' and then different topology of the 'NC-domain', therefore residues at position 58 are believed to function as structure and bioactivity switch for specificity of scorpion alpha-toxins. The mechanism for stabilizing the geometry of the 'NC-domain' in wide-type scorpion alpha-toxins is also discussed.

PubMed: 19932686
DOI: 10.1016/j.bbrc.2009.11.110

実験手法

SOLUTION NMR