8BO0
Solution structure of Lqq4 toxin from Leiurus quinquestriatus quinquestriatus
Summary for 8BO0
| Entry DOI | 10.2210/pdb8bo0/pdb |
| NMR Information | BMRB: 34771 |
| Descriptor | Alpha-toxin Lqq4 (1 entity in total) |
| Functional Keywords | toxin, protein |
| Biological source | Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 7211.23 |
| Authors | Mineev, K.S.,Motov, V.V.,Vassilevski, A.A.,Chernykh, M.A.,Kuzmenkov, A.I. (deposition date: 2022-11-14, release date: 2023-09-20, Last modification date: 2023-10-04) |
| Primary citation | 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 Cited by 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: 37501371DOI: 10.1002/1873-3468.14705 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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