7NMQ
Bacillus cereus HblL1 toxin component
Summary for 7NMQ
| Entry DOI | 10.2210/pdb7nmq/pdb |
| Descriptor | Hemolysin BL lytic component L1, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | bacillus cereus, toxin, haemolysin bl, alpha helical pore forming toxin |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 39974.08 |
| Authors | Rizkallah, P.J.,Berry, C. (deposition date: 2021-02-23, release date: 2021-04-07, Last modification date: 2024-01-31) |
| Primary citation | Worthy, H.L.,Williamson, L.J.,Auhim, H.S.,Leppla, S.H.,Sastalla, I.,Jones, D.D.,Rizkallah, P.J.,Berry, C. The Crystal Structure of Bacillus cereus HblL 1 . Toxins, 13:-, 2021 Cited by PubMed Abstract: The Hbl toxin is a three-component haemolytic complex produced by strains and implicated as a cause of diarrhoea in food poisoning. While the structure of the HblB component of this toxin is known, the structures of the other components are unresolved. Here, we describe the expression of the recombinant HblL component and the elucidation of its structure to 1.36 Å. Like HblB, it is a member of the alpha-helical pore-forming toxin family. In comparison to other members of this group, it has an extended hydrophobic beta tongue region that may be involved in pore formation. Molecular docking was used to predict possible interactions between HblL and HblB, and suggests a head to tail dimer might form, burying the HblL beta tongue region. PubMed: 33807365DOI: 10.3390/toxins13040253 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.36 Å) |
Structure validation
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