ArticleProceedings of the National Academy of Sciences of the United States of America1998
The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Characterization of Cry4Aa Toxin fromInsects · 2025Article
- Essential Role of Non-Conserved α4-HisProtein and peptide letters · 2025Article
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- Molecular architecture of black widow spider neurotoxins.Nature communications · 2021Article
- Rearrangement of N-Terminal α-Helices ofToxins · 2020Article
- Review
- Modification of Cry4Aa toward Improved Toxin Processing in the Gut of the Pea Aphid, Acyrthosiphon pisum.PloS one · 2016Article
- Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS.The Journal of biological chemistry · 2015Article
- Review
- Article
- Structural analysis and molecular dynamics simulations of novel δ-endotoxin Cry1Id from Bacillus thuringiensis to pave the way for development of novel fusion proteins against insect pests of crops.Journal of molecular modeling · 2013Article
- Role of pore-forming toxins in bacterial infectious diseases.Microbiology and molecular biology reviews : MMBR · 2013Review
- Electrical hypothesis of toxicity of the Cry toxins for mosquito larvae.Bioscience reports · 2013Article
- In silico modeling and functional interpretations of Cry1Ab15 toxin from Bacillus thuringiensis BtB-Hm-16.BioMed research international · 2013Article
- Article
- Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from Bacillus thuringiensis AC11.Indian journal of microbiology · 2012Article
- Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane.The Journal of biological chemistry · 2011Article
- Novel Bacillus thuringiensis δ-endotoxin active against Locusta migratoria manilensis.Applied and environmental microbiology · 2011Article
- Effects of mutations within surface-exposed loops in the pore-forming domain of the Cry9Ca insecticidal toxin of Bacillus thuringiensis.The Journal of membrane biology · 2010Article
- Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis.The Journal of general physiology · 2010Article
Corrections and comments
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4 authors.
Funding
Abstract
The aim of this study was to elucidate the mechanism of membrane insertion and the structural organization of pores formed by Bacillus thuringiensis delta-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 with the bilayer membrane was also probed by a Monte Carlo simulation protocol to determine lowest-energy orientations. Our results are consistent with a situation in which helices alpha4 and alpha5 insert into the membrane as a helical hairpin in an antiparallel manner, while the other helices lie on the membrane surface like the ribs of an umbrella (the "umbrella model"). Our results also support the suggestion that alpha7 may serve as a binding sensor to initiate the structural rearrangement of the pore-forming domain.
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