Ovine β-lactoglobulin at atomic resolution.
The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.
Structural Biochemistry Group, Institute of Cell and Molecular Biology, The University of Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh EH10 3BF, Scotland.
George
G
Kontopidis
Structural Biochemistry Group, Institute of Cell and Molecular Biology, The University of Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh EH10 3BF, Scotland.
Anna
A
Nordle Gilliver
Structural Biochemistry Group, Institute of Cell and Molecular Biology, The University of Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh EH10 3BF, Scotland.
Lindsay
L
Sawyer
D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D007782:Lactoglobulins / Q000737:chemistry* / Q000302:isolation & purification*; D008894:Milk Proteins / Q000737:chemistry / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012756:Sheep
D007782:Lactoglobulins; D008894:Milk Proteins
Ovis aries; ovine β-lactoglobulin