2NRJ

Crystal Structure of Hemolysin binding component from Bacillus cereus

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 

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


Literature

X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus

Madegowda, M., Eswaramoorthy, S., Burley, S.K., Swaminathan, S.

(2008) Proteins 71: 534-540

  • DOI: https://doi.org/10.1002/prot.21888
  • Primary Citation of Related Structures:  
    2NRJ

  • PubMed Abstract: 

    Bacillus cereus Hemolysin BL enterotoxin, a ternary complex of three proteins, is the causative agent of food poisoning and requires all three components for virulence. The X-ray structure of the binding domain of HBL suggests that it may form a pore similar to other soluble channel forming proteins. A putative pathway of pore formation is discussed.

    • Organizational Affiliation: 

    Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hbl B protein346Bacillus cereusMutation(s): 7 
Gene Names: hblA
UniProt
Find proteins for P80172 (Bacillus cereus)
Explore P80172 
Go to UniProtKB:  P80172
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80172
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 127.833α = 90
b = 28.549β = 105.01
c = 89.738γ = 90
Software Package:
Software NamePurpose
CNSrefinement
CBASSdata collection
HKL-3000data reduction
HKL-3000data scaling
SHARPphasing
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-11-14
    Type: Initial release
  • Version 1.1: 2008-04-21
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-02-03
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references