4NLJ: Crystal Structure Of Sheep Beta-lactoglobulin (space Group P1)

Ovine beta-lactoglobulin has been isolated from whey fraction of sheep milk and crystallized. The high-resolution structures of two crystal forms (triclinic and trigonal) obtained at pH 7.0 have been determined revealing that ovine protein, similarly to its bovine analog, is dimeric. Access to the binding site located in the eight-stranded antiparallel beta-barrel in both structures is blocked by the EF loop that has been found in closed conformation. Similarly to bovine lactoglobulin (BLG), conformation of the EF loop is stabilized by hydrogen bond between Glu89 and Ser116 indicating that Tanford transition might occur with the same mechanism. The substitution at six positions in relation to the most abundant isoform B of BLG also affects the distribution of electrostatic potentials and the total charge. (c) 2014 Wiley Periodicals, Inc. Biopolymers 101: 886-894, 2014.
PDB ID: 4NLJDownload
MMDB ID: 118288
PDB Deposition Date: 2013/11/14
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 1.4  Å
Source Organism:
Similar Structures:
Biological Unit for 4NLJ: dimeric; determined by author and by software (PISA)
Molecular Components in 4NLJ
Label Count Molecule
Proteins (2 molecules)
Beta-lactoglobulin-1/b(Gene symbol: PAEP)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB