Structurally conserved aromaticity of Tyr249 and Phe 264 in helix 7 is important for toxicity of the Bacillus thuringiensis Cry4Ba toxin
Functional elements of the conserved helix 7 in the poreforming domain of the Bacillus thuringiensis Cry δ-endotoxins have not yet been clearly identified. Here, we initially performed alanine substitutions of four highly conserved aromatic residues, Trp243, Phe246, Tyr 249 and Phe264, in helix 7 of...
Saved in:
| Main Authors: | , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Published: |
2018
|
| Subjects: | |
| Online Access: | https://repository.li.mahidol.ac.th/handle/123456789/24234 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Institution: | Mahidol University |