4TLJ

Ultra-high resolution crystal structure of caprine Beta-lactoglobulin

Summary for 4TLJ

• Entry DOI: 10.2210/pdb4tlj/pdb
• Descriptor: Beta-lactoglobulin, 1,4-BUTANEDIOL (3 entities in total)
• Functional Keywords: beta barrel, lipocalin, transport protein
• Biological source: Capra hircus (Goat)
• Cellular location: Secreted: P02756
• Total number of polymer chains: 2
• Total formula weight: 36514.50

Authors

Crowther, J.M.,Jameson, G.B.,Suzuki, H.,Dobson, R.C.J. (deposition date: 2014-05-30, release date: 2014-06-18, Last modification date: 2024-10-23)

Primary citation

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.
Ultra-high resolution crystal structure of recombinant caprine beta-lactoglobulin.
Febs Lett., 588:3816-3822, 2014

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.

PubMed: 25241165
DOI: 10.1016/j.febslet.2014.09.010

Experimental method

X-RAY DIFFRACTION (1.17 Å)