4TLJ

Ultra-high resolution crystal structure of caprine Beta-lactoglobulin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.17 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.132 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history. 


Literature

Ultra-high resolution crystal structure of recombinant caprine beta-lactoglobulin.

Crowther, J.M., Lasse, M., Suzuki, H., Kessans, S.A., Loo, T.S., Norris, G.E., Hodgkinson, A.J., Jameson, G.B., Dobson, R.C.

(2014) FEBS Lett 588: 3816-3822

  • DOI: https://doi.org/10.1016/j.febslet.2014.09.010
  • Primary Citation of Related Structures:  
    4TLJ

  • PubMed Abstract: 

    β-Lactoglobulin (βlg) is the most abundant whey protein in the milks of ruminant animals. While bovine βlg has been subjected to a vast array of studies, little is known about the caprine ortholog. We present an ultra-high resolution crystal structure of caprine βlg complemented by analytical ultracentrifugation and small-angle X-ray scattering data. In both solution and crystalline states caprine βlg is dimeric (K(D)<5 μM); however, our data suggest a flexible quaternary arrangement of subunits within the dimer. These structural findings will provide insight into relationships among structural, processing, nutritional and immunological characteristics that distinguish cow's and goat's milk.

    • Organizational Affiliation: 

    Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactoglobulin
A, B
162Capra hircusMutation(s): 0 
Gene Names: LGB
UniProt
Find proteins for P02756 (Capra hircus)
Explore P02756 
Go to UniProtKB:  P02756
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02756
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BU1
Query on BU1
Download Ideal Coordinates CCD File 
C [auth A]1,4-BUTANEDIOL
C4 H10 O2
WERYXYBDKMZEQL-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.17 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.132 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.32α = 90
b = 54.58β = 107.31
c = 56.39γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
Cootmodel building

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-06-18
    Type: Initial release
  • Version 1.1: 2014-10-15
    Changes: Database references
  • Version 1.2: 2014-12-24
    Changes: Database references
  • Version 1.3: 2015-02-04
    Changes: Derived calculations
  • Version 2.0: 2017-11-22
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description, Source and taxonomy
  • Version 2.1: 2023-09-27
    Changes: Data collection, Database references, Refinement description