publication . Other literature type . 1998

The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an “umbrella-like” structure of the pore

Gazit, Ehud; Rocca, Paolo La; Sansom, Mark S. P.; Shai, Yechiel;
Open Access English
  • Published: 13 Oct 1998
  • Publisher: The National Academy of Sciences
Abstract
The aim of this study was to elucidate the mechanism of membrane insertion and the structural organization of pores formed by Bacillus thuringiensis δ-endotoxin. We determined the relative affinities for membranes of peptides corresponding to the seven helices that compose the toxin pore-forming domain, their modes of membrane interaction, their structures within membranes, and their orientations relative to the membrane normal. In addition, we used resonance energy transfer measurements of all possible combinatorial pairs of membrane-bound helices to map the network of interactions between helices in their membrane-bound state. The interaction of the helices wi...
Subjects
free text keywords: Biological Sciences
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Other literature type . 1998
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