5IO7

Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.254 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Investigation of high pressure effect on the structure and adsorption of beta-lactoglobulin.

Kurpiewska, K.Biela, A.Loch, J.I.Swiatek, S.Jachimska, B.Lewinski, K.

(2017) Colloids Surf B Biointerfaces 161: 387-393

  • DOI: https://doi.org/10.1016/j.colsurfb.2017.10.069
  • Primary Citation of Related Structures:  
    5IO5, 5IO6, 5IO7

  • PubMed Abstract: 

    β-Lactoglobulin, being one of the principal whey protein, is of huge importance to the food industry. Temperature/pressure effects on this small protein has been extensively studied by industry. To characterize biochemical properties of β-lactoglobulin after or during pressurization, a wide range of methods have been used thus far. In this study, for the first time, the pressure-induced conformation of β-lactoglobulin in the crystal state was determined, at pressure 430 MPa. Changes observed in the high pressure structure correlate with the physico-chemical properties of pressure-treated β-lactoglobulin obtained from dynamic light scattering, electrophoretic mobility and quartz crystal microbalance with dissipation monitoring measurements. A comparison between the β-lactoglobulin structures determined at both high and ambient pressure contrasts the stable nature of the protein core and adjacent loop fragments. At high pressure the β-lactoglobulin structure presents early signs of dimer dissociation, charge and conformational changes characteristic for initial unfolded intermediate as well as a significant modification of the binding pocket volume. Those observations are supported by changes in zeta potential values and results in increase affinity of the β-lactoglobulin adsorption onto gold surface. Observed pressure-induced structural modifications were previously suggested as an important factor contributing to β-lactoglobulin denaturation process. Presented studies provide detailed analysis of pressure-associated structural changes influencing β-lactoglobulin conformation and consequently its adsorption.


  • Organizational Affiliation

    Jagiellonian University, Faculty of Chemistry, Department of Crystal Chemistry and Crystal Physics, Biocrystallography Group, 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
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.254 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.073α = 90
b = 53.073β = 90
c = 111.722γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
Cootmodel building

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
European Regional Development FundPolandPOIG.02.01.00-12-023/08

Revision History  (Full details and data files)

  • Version 1.0: 2016-03-16
    Type: Initial release
  • Version 1.1: 2017-11-15
    Changes: Database references
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Refinement description