Helix 4 Mutants of the Bacillus thuringiensis Insecticidal Toxin Cry1Aa Display Altered Pore-Forming Abilities

The role played by α-helix 4 of the Bacillus thuringiensis toxin Cry1Aa in pore formation was investigated by individually replacing each of its charged residues with either a neutral or an oppositely charged amino acid by using site-directed mutagenesis. The majority of the resulting mutant protein...

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Autors principals: Vachon, Vincent, Préfontaine, Gabrielle, Rang, Cécile, Coux, Florence, Juteau, Marc, Schwartz, Jean-Louis, Brousseau, Roland, Frutos, Roger, Laprade, Raynald, Masson, Luke
Format: Artigo
Idioma:Inglês
Publicat: American Society for Microbiology 2004
Matèries:
Invertebrate Microbiology
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC522081/
https://ncbi.nlm.nih.gov/pubmed/15466558
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.70.10.6123-6130.2004
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