Toxic principle of selva ant venom is a pore‐forming protein transformer

FEBS Letters

Sobol, A.G.¹  Sukhanov, S.V.¹  Arseniev, A.S.¹  Grishin, E.V.¹  Torgov, M.Yu.¹  Nolde, D.E.¹  Pluzhnikov, K.A.¹ 

[1] Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16/10, 117871 Moscow, Russian Federation

关键词: Ant venom;    Ectatomin;    Structure;    Pore-forming protein;    Ectatomma tuberculatum;    Ea;    ectatomin;    2D;    two-dimensional;    COSY;    2D homonuclear correlated spectroscopy;    NOESY;    2 D homonuclear NOE spectroscopy;    TOCSY;    2 D homonuclear total correlation spectroscopy;    RMSD;    root mean square deviation;   

DOI  :  10.1016/0014-5793(94)00518-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-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.

【 授权许可】

Unknown