6FXB
Bovine beta-lactoglobulin variant A at pH 4.0
Summary for 6FXB
Entry DOI | 10.2210/pdb6fxb/pdb |
Descriptor | Major allergen beta-lactoglobulin, NITRATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | lactoglobulin, milk protein, allergen |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 4 |
Total formula weight | 73779.19 |
Authors | Khan, S.,Ipsen, R.,Almdal, K.,Svensson, B.,Harris, P. (deposition date: 2018-03-08, release date: 2018-05-23, Last modification date: 2024-10-23) |
Primary citation | Khan, S.,Ipsen, R.,Almdal, K.,Svensson, B.,Harris, P. Revealing the Dimeric Crystal and Solution Structure of beta-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer-Dimer Equilibrium. Biomacromolecules, 19:2905-2912, 2018 Cited by PubMed Abstract: The dimeric structure of bovine β-lactoglobulin A (BLGA) at pH 4.0 was solved to 2.0 Å resolution. Fitting the BLGA pH 4.0 structure to SAXS data at low ionic strength (goodness of fit R-factor = 3.6%) verified the dimeric state in solution. Analysis of the monomer-dimer equilibrium at varying pH and ionic strength by SAXS and scattering modeling showed that BLGA is dimeric at pH 3.0 and 4.0, shifting toward a monomer at pH 2.2, 2.6, and 7.0 yielding monomer/dimer ratios of 80/20%, 50/50%, and 25/75%, respectively. BLGA remained a dimer at pH 3.0 and 4.0 in 50-150 mM NaCl, whereas the electrostatic shielding raised the dimer content at pH 2.2, 2.6, and 7.0, i.e., below and above the pI. Overall, the findings provide new insights into the molecular characteristics of BLGA relevant for dairy product formulations and for various biotechnological and pharmaceutical applications. PubMed: 29737841DOI: 10.1021/acs.biomac.8b00471 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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