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8PWT

Solution structure of the peptide U11-MYRTX-Tb1a from the venom of the ant Tetramorium bicarinatum

Summary for 8PWT
Entry DOI10.2210/pdb8pwt/pdb
NMR InformationBMRB: 34837
DescriptorU11-myrmicitoxin-Tb1a (1 entity in total)
Functional Keywordsant venom peptide, neurotoxin, tetramorium, helix peptide, toxin
Biological sourceTetramorium bicarinatum
Total number of polymer chains1
Total formula weight4033.89
Authors
Jouvensal, L.,Paquet, F.,Loth, K. (deposition date: 2023-07-21, release date: 2023-10-25, Last modification date: 2024-10-16)
Primary citationBarasse, V.,Jouvensal, L.,Boy, G.,Billet, A.,Ascoet, S.,Lefranc, B.,Leprince, J.,Dejean, A.,Lacotte, V.,Rahioui, I.,Sivignon, C.,Gaget, K.,Ribeiro Lopes, M.,Calevro, F.,Da Silva, P.,Loth, K.,Paquet, F.,Treilhou, M.,Bonnafe, E.,Touchard, A.
Discovery of an Insect Neuroactive Helix Ring Peptide from Ant Venom.
Toxins, 15:-, 2023
Cited by
PubMed Abstract: Ants are among the most abundant terrestrial invertebrate predators on Earth. To overwhelm their prey, they employ several remarkable behavioral, physiological, and biochemical innovations, including an effective paralytic venom. Ant venoms are thus cocktails of toxins finely tuned to disrupt the physiological systems of insect prey. They have received little attention yet hold great promise for the discovery of novel insecticidal molecules. To identify insect-neurotoxins from ant venoms, we screened the paralytic activity on blowflies of nine synthetic peptides previously characterized in the venom of . We selected peptide U, a 34-amino acid peptide, for further insecticidal, structural, and pharmacological experiments. Insecticidal assays revealed that U is one of the most paralytic peptides ever reported from ant venoms against blowflies and is also capable of paralyzing honeybees. An NMR spectroscopy of U uncovered a unique scaffold, featuring a compact triangular ring helix structure stabilized by a single disulfide bond. Pharmacological assays using S2 cells demonstrated that U is not cytotoxic, but suggest that it may modulate potassium conductance, which structural data seem to corroborate and will be confirmed in a future extended pharmacological investigation. The results described in this paper demonstrate that ant venom is a promising reservoir for the discovery of neuroactive insecticidal peptides.
PubMed: 37888631
DOI: 10.3390/toxins15100600
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237992

数据于2025-06-25公开中

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