The equinatoxin N-terminus is transferred across planar lipid membranes and helps to stabilize the transmembrane pore.
作者： Katarina Kristan , Gabriella Viero , Peter Mac̆ek , Mauro Dalla Serra , Gregor Anderluh
DOI: 10.1111/J.1742-4658.2006.05608.X
关键词:
摘要: Equinatoxin II is a cytolytic protein isolated from the sea anemone Actinia equina. It member of actinoporins, family eukaryotic pore-forming toxins with unique mechanism pore formation. 20 kDa cysteineless protein, sphingomyelin-dependent activity. Recent studies showed that N-terminal region molecule requires conformational flexibility during An understanding position in final and its role membrane insertion stability essential to define precise molecular The formation pores their electrophysiologic characteristics were studied planar lipid membranes. We show amino acids at positions 1 3 equinatoxin are exposed lumen pore. Moreover, sulfhydryl reagents hexa-histidine tag attached N-terminus revealed toxin extends through other (trans) side negatively charged residues inside crucial channel. Finally, we detected new, less stable, state lower conductance by using deletion mutant which first five removed. propose help anchor amphipathic helix on trans consequently stabilize transmembrane
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