7AY8

NMR solution structure of Tbo-IT2

7AY8 の概要

• エントリーDOI: 10.2210/pdb7ay8/pdb
• NMR情報: BMRB: 34574
• 分子名称: Tbo-IT2 (1 entity in total)
• 機能のキーワード: protein, toxin
• 由来する生物種: Tibellus oblongus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4220.97

構造登録者

Mineev, K.S.,Kornilov, F.D.,Lushpa, V.A.,Korolkova, Y.A.,Maleeva, E.E.,Andreev, Y.A.,Kozlov, S.A.,Arseniev, A.S. (登録日: 2020-11-11, 公開日: 2021-03-03, 最終更新日: 2024-11-20)

主引用文献

Korolkova, Y.,Maleeva, E.,Mikov, A.,Lobas, A.,Solovyeva, E.,Gorshkov, M.,Andreev, Y.,Peigneur, S.,Tytgat, J.,Kornilov, F.,Lushpa, V.,Mineev, K.,Kozlov, S.
New Insectotoxin from Tibellus Oblongus Spider Venom Presents Novel Adaptation of ICK Fold.
Toxins, 13:-, 2021

PubMed Abstract: The spider is an active predator that does not spin webs and remains poorly investigated in terms of venom composition. Here, we present a new toxin, named Tbo-IT2, predicted by cDNA analysis of venom glands transcriptome. The presence of Tbo-IT2 in the venom was confirmed by proteomic analyses using the LC-MS and MS/MS techniques. The distinctive features of Tbo-IT2 are the low similarity of primary structure with known animal toxins and the unusual motif of 10 cysteine residues distribution. Recombinant Tbo-IT2 (rTbo-IT2), produced in using the thioredoxin fusion protein strategy, was structurally and functionally studied. rTbo-IT2 showed insecticidal activity on larvae of the housefly (LD 200 μg/g) and no activity on the panel of expressed neuronal receptors and ion channels. The spatial structure of the peptide was determined in a water solution by NMR spectroscopy. The Tbo-IT2 structure is a new example of evolutionary adaptation of a well-known inhibitor cystine knot (ICK) fold to 5 disulfide bonds configuration, which determines additional conformational stability and gives opportunities for insectotoxicity and probably some other interesting features.

PubMed: 33406803
DOI: 10.3390/toxins13010029

実験手法

SOLUTION NMR