Toxins · 2021
The Crystal Structure of Bacillus cereus HblL1.
СтатьяResearch Support, N.I.H., IntramuralПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Worthy Harley L, Williamson Lainey J, Auhim Husam Sabah, Leppla Stephen H, Sastalla Inka, Jones D Dafydd, Rizkallah Pierre J, Berry Colin
Аннотация
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.
Предметные рубрики MeSH
Bacillus cereusBacterial ProteinsHemolysin ProteinsHydrophobic and Hydrophilic InteractionsMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein MultimerizationRecombinant ProteinsStructure-Activity Relationship