5MOU
NMR spatial structure of scorpion alpha-like toxin BeM9
Summary for 5MOU
| Entry DOI | 10.2210/pdb5mou/pdb |
| NMR Information | BMRB: 34078 |
| Descriptor | Alpha-mammal toxin BeM9 (1 entity in total) |
| Functional Keywords | protein neurotoxin, protein |
| Biological source | Mesobuthus eupeus (Lesser Asian scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 7351.35 |
| Authors | Mineev, K.S.,Kuldushev, N.A.,Berkut, A.A.,Grishin, E.V.,Vassilevski, A.A.,Arseniev, A.S. (deposition date: 2016-12-14, release date: 2018-01-17, Last modification date: 2024-11-13) |
| Primary citation | Kuldyushev, N.A.,Mineev, K.S.,Berkut, A.A.,Peigneur, S.,Arseniev, A.S.,Tytgat, J.,Grishin, E.V.,Vassilevski, A.A. Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels. Proteins, 86:1117-1122, 2018 Cited by PubMed Abstract: Sodium channel alpha-toxins from scorpion venom (α-NaTx) inhibit the inactivation of voltage-gated sodium channels. We used solution NMR to investigate the structure of BeM9 toxin from Mesobuthus eupeus scorpion, a prototype α-NaTx classified as an "α-like" toxin due to its wide spectrum of activity on insect and mammalian channels. We identified a new motif that we named "arginine hand," whereby arginine side chain forms several hydrogen bonds with main chain atoms. The arginine hand was found in the "specificity module," a part of the molecule that dictates toxin selectivity; and just single arginine-to-lysine point mutation drastically changed BeM9 selectivity profile. PubMed: 30007037DOI: 10.1002/prot.25583 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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