5LKE

Bovine beta-lactoglobulin complex with myristic acid, ambient pressure


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.193 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Towards understanding the effect of high pressure on food protein allergenicity: beta-lactoglobulin structural studies.

Kurpiewska, K.Biela, A.Loch, J.I.Lipowska, J.Siuda, M.Lewinski, K.

(2019) Food Chem 270: 315-321

  • DOI: https://doi.org/10.1016/j.foodchem.2018.07.104
  • Primary Citation of Related Structures:  
    5LKE, 5LKF

  • PubMed Abstract: 

    A number of studies were devoted to understanding an immunological effect of pressure-treated β-lactoglobulin. In our previous work we have proved that high pressure significantly modifies β-lactoglobulin conformation and consequently its physicochemical properties. Here, structure of β-lactoglobulin complex with myristic acid determined at the highest accepted by the crystal pressure value of 550 MPa is reported. Our results structurally prove that pressure noticeably modifies positions of the major β-lactoglobulin epitopes. Considering the biological impact of observed changes in epitope regions, high pressure β-lactoglobulin structure presents a step forward in understanding the pressure modification of food protein allergenicity. The conformational changes of pressurized β-lactoglobulin did not support the hypothesis that proteolytic digestion facilitated by pressure is caused by an exposure of the digestive sites. Our findings demonstrate that high pressure protein crystallography can potentially identify the most pressure-sensitive fragments in allergens, and can therefore support development of hypoallergenic food products.


  • Organizational Affiliation

    Jagiellonian University, Faculty of Chemistry, Department of Crystal Chemistry and Crystal Physics, Gronostajowa 2, 30-387 Kraków, Poland; Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, Poland. Electronic address: kurpiews@chemia.uj.edu.pl.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactoglobulin162Bos taurusMutation(s): 0 
UniProt
Find proteins for P02754 (Bos taurus)
Explore P02754 
Go to UniProtKB:  P02754
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02754
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
MYR
Query on MYR

Download Ideal Coordinates CCD File 
B [auth A]MYRISTIC ACID
C14 H28 O2
TUNFSRHWOTWDNC-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.313 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.193 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.179α = 90
b = 54.179β = 90
c = 112.916γ = 120
Software Package:
Software NamePurpose
Aimlessdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
CrysalisProdata reduction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-08-10
    Type: Initial release
  • Version 1.1: 2019-05-08
    Changes: Data collection, Database references
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Refinement description