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1G92

SOLUTION STRUCTURE OF PONERATOXIN

Summary for 1G92
Entry DOI10.2210/pdb1g92/pdb
NMR InformationBMRB: 4921
DescriptorPONERATOXIN (1 entity in total)
Functional Keywordstoxin; neurotoxin; sodium channel inhibitor, toxin
Total number of polymer chains1
Total formula weight2759.36
Authors
Szolajska, E.,Poznanski, J.,Ferber, M.L.,Michalik, J.,Gout, E.,Fender, P.,Bailly, I.,Dublet, B.,Chroboczek, J. (deposition date: 2000-11-22, release date: 2003-11-18, Last modification date: 2024-05-22)
Primary citationSzolajska, E.,Poznanski, J.,Ferber, M.L.,Michalik, J.,Gout, E.,Fender, P.,Bailly, I.,Dublet, B.,Chroboczek, J.
Poneratoxin, a neurotoxin from ant venom. Structure and expression in insect cells and construction of a bio-insecticide.
Eur.J.Biochem., 271:2127-2136, 2004
Cited by
PubMed Abstract: Poneratoxin is a small neuropeptide found in the venom of the ant Paraponera clavata. It is stored in the venom reservoir as an inactive 25-residue peptide. Here we describe both chemically synthesized poneratoxin and poneratoxin obtained by expression in insect cells. When expressed in insect cells, poneratoxin was observed attached to cell membranes. Both synthetic and recombinant ponerotoxins were soluble below pH 4.5. The structure of synthetic poneratoxin was characterized by circular dichroism and solved by nuclear magnetic resonance. In an environment imitating a lipid bilayer, at pH within the range of insect hemolymph, synthetic poneratoxin has a V shape, with two alpha-helices connected by a beta-turn. Insect larvae were paralyzed by injection of either of the purified toxins, with the recombinant one acting faster. The recombinant toxin-producing baculovirus reduced the average survival time of the insect host by 25 h compared with unmodified virus. Mass spectrometry analysis showed that the recombinant toxin has an N-terminal 21-residue extension, possibly improving its stability and/or stabilizing the membrane-bound state. The potential use of poneratoxin for the construction of biological insecticide is discussed.
PubMed: 15153103
DOI: 10.1111/j.1432-1033.2004.04128.x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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