Structural highlights
Function
Q1XBV1_BACCE
Publication Abstract from PubMed
The Hbl toxin is a three-component haemolytic complex produced by Bacillus cereus sensu lato strains and implicated as a cause of diarrhoea in B. cereus 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 HblL1 component and the elucidation of its structure to 1.36 A. 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 HblL1 and HblB, and suggests a head to tail dimer might form, burying the HblL1 beta tongue region.
The Crystal Structure of Bacillus cereus HblL1.,Worthy HL, Williamson LJ, Auhim HS, Leppla SH, Sastalla I, Jones DD, Rizkallah PJ, Berry C Toxins (Basel). 2021 Mar 31;13(4). pii: toxins13040253. doi:, 10.3390/toxins13040253. PMID:33807365[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Worthy HL, Williamson LJ, Auhim HS, Leppla SH, Sastalla I, Jones DD, Rizkallah PJ, Berry C. The Crystal Structure of Bacillus cereus HblL1. Toxins (Basel). 2021 Mar 31;13(4). pii: toxins13040253. doi:, 10.3390/toxins13040253. PMID:33807365 doi:http://dx.doi.org/10.3390/toxins13040253
