7NMQ

Bacillus cereus HblL1 toxin component

  • Classification: TOXIN
  • Organism(s): Bacillus cereus
  • Expression System: Bacillus anthracis
  • Mutation(s): No 

  • Deposited: 2021-02-23 Released: 2021-04-07 
  • Deposition Author(s): Rizkallah, P.J., Berry, C.
  • Funding Organization(s): Biotechnology and Biological Sciences Research Council (BBSRC), National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.162 
  • R-Value Observed: 0.164 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

The Crystal Structure of Bacillus cereus HblL 1 .

Worthy, H.L., Williamson, L.J., Auhim, H.S., Leppla, S.H., Sastalla, I., Jones, D.D., Rizkallah, P.J., Berry, C.

(2021) Toxins (Basel) 13

  • DOI: https://doi.org/10.3390/toxins13040253
  • Primary Citation of Related Structures:  
    7NMQ

  • PubMed 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 HblL 1 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 1 and HblB, and suggests a head to tail dimer might form, burying the HblL 1 beta tongue region.

    • Organizational Affiliation: 

    School of Biosciences, Cardiff University, Park Place, Cardiff CF10 3AX, UK.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hemolysin BL lytic component L1365Bacillus cereusMutation(s): 0 
Gene Names: 
UniProt
Find proteins for Q1XBV1 (Bacillus cereus)
Explore Q1XBV1 
Go to UniProtKB:  Q1XBV1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1XBV1
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.162 
  • R-Value Observed: 0.164 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 36.66α = 90
b = 72.96β = 90
c = 133.05γ = 90
Software Package:
Software NamePurpose
Aimlessdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
xia2data reduction
XDSdata reduction

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research Council (BBSRC)United KingdomBB/M009122/1
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2021-04-07
    Type: Initial release
  • Version 1.1: 2021-04-14
    Changes: Database references
  • Version 1.2: 2021-04-21
    Changes: Database references, Structure summary
  • Version 1.3: 2021-04-28
    Changes: Database references
  • Version 1.4: 2024-01-31
    Changes: Data collection, Database references, Refinement description