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The Crystal Structure of Bacillus cereus HblL₁.

ABSTRACT: 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 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 HblL₁ and HblB, and suggests a head to tail dimer might form, burying the HblL₁ beta tongue region.

SUBMITTER: Worthy HL

PROVIDER: S-EPMC8065917 | biostudies-literature |

REPOSITORIES: biostudies-literature

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