8HHE
Crystal structure of Cry5B from Bacillus thuringiensis at 4.5 A resolution
Summary for 8HHE
| Entry DOI | 10.2210/pdb8hhe/pdb |
| Descriptor | Crystaline entomocidal protoxin (1 entity in total) |
| Functional Keywords | bacillus thuringiensis, cry protein, nematicidal protein, toxin |
| Biological source | Bacillus thuringiensis YBT-1518 |
| Total number of polymer chains | 2 |
| Total formula weight | 181221.66 |
| Authors | Li, J.,Chan, M.K. (deposition date: 2022-11-16, release date: 2022-12-07, Last modification date: 2024-11-06) |
| Primary citation | Li, J.,Wang, L.,Kotaka, M.,Lee, M.M.,Chan, M.K. Insights from the Structure of an Active Form of Bacillus thuringiensis Cry5B. Toxins, 14:-, 2022 Cited by PubMed Abstract: The crystal protein Cry5B, a pore-forming protein produced by the soil bacterium , has been demonstrated to have excellent anthelmintic activity. While a previous structure of the three-domain core region of Cry5B(112-698) had been reported, this structure lacked a key N-terminal extension critical to function. Here we report the structure of Cry5B(27-698) containing this N-terminal extension. This new structure adopts a distinct quaternary structure compared to the previous Cry5B(112-698) structure, and also exhibits a change in the conformation of residues 112-140 involved in linking the N-terminal extension to the three-domain core by forming a random coil and an extended α-helix. A role for the N-terminal extension is suggested based on a computational model of the tetramer with the conformation of residues 112-140 in its alternate α-helix conformation. Finally, based on the Cry5B(27-698) structure, site-directed mutagenesis studies were performed on Tyr495, which revealed that having an aromatic group or bulky group at this residue 495 is important for Cry5B toxicity. PubMed: 36548720DOI: 10.3390/toxins14120823 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.5 Å) |
Structure validation
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