Ectatomin (Ea) is a newly isolated main toxic component of Ectatomma tuberculatum ant venom. Structural and electrophysiological studies were performed with purified Ea. The protein consists of two homologous polypeptide chains (37 and 34 residues) and forms a four alpha-helix bundle in aqueous solution. On insertion into artificial bilayer membranes, two Ea molecules form an ion pore. Our results suggest that the 'inside-out' mechanism of pore formation requires a significant movement of Ea helical parts. The pore formation in the cell membrane might well explain the toxic activity of Ea, not excluding at the same time its intracellular activities.
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Ectatomin (Ea) is a newly isolated main toxic component of Ectatomma tuberculatum ant venom. Structural and electrophysiological studies were performed with purified Ea. The protein consists of two homologous polypeptide chains (37 and 34 residues) and forms a four alpha-helix bundle in aqueous solution. On insertion into artificial bilayer membranes, two Ea molecules form an ion pore. Our results suggest that the 'inside-out' mechanism of pore formation requires a significant movement of Ea helical parts. The pore formation in the cell membrane might well explain the toxic activity of Ea, not excluding at the same time its intracellular activities.
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| uniprot:name |
FEBS Lett.
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| uniprot:author |
Arseniev A.S.,
Grishin E.V.,
Nolde D.E.,
Pluzhnikov K.A.,
Sobol A.G.,
Sukhanov S.V.,
Torgov M.Y.
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| uniprot:date |
1994
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| uniprot:pages |
112-116
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| uniprot:title |
Toxic principle of selva ant venom is a pore-forming protein transformer.
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| uniprot:volume |
347
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| dc-term:identifier |
doi:10.1016/0014-5793(94)00518-4
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