Publication
Article Metrics
Citations
Online attention
The crystal structure of Bacillus cereus HblL1
Authors:
Harley L.
Worthy
(Cardiff University; Exeter University)
,
Lainey J.
Williamson
(Cardiff University)
,
Husam Sabah
Auhim
(Cardiff University; University of Baghdad)
,
Stephen H.
Leppla
(National Institute of Allergy and Infectious Diseases, National Institutes of Health)
,
Inka
Sastalla
(National Institute of Allergy and Infectious Diseases, National Institutes of Health)
,
D. Dafydd
Jones
(Cardiff University)
,
Pierre J.
Rizkallah
(Cardiff University)
,
Colin
Berry
(Cardiff University)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Toxins
, VOL 13
State:
Published (Approved)
Published:
March 2021
Diamond Proposal Number(s):
18812

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.
Journal Keywords: tripartite toxin; hemolytic toxin; haemolytic toxin; Bacillus cereus
Diamond Keywords: Bacteria
Subject Areas:
Biology and Bio-materials
Instruments:
I04-1-Macromolecular Crystallography (fixed wavelength)
Added On:
06/04/2021 10:37
Discipline Tags:
Pathogens
Health & Wellbeing
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)