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Ovine ?-lactoglobulin at atomic resolution.

ABSTRACT: The crystal structure of the triclinic form of the milk protein ?-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.

SUBMITTER: Kontopidis G 

PROVIDER: S-EPMC4231851 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Ovine β-lactoglobulin at atomic resolution.

Kontopidis George G   Nordle Gilliver Anna A   Sawyer Lindsay L  

Acta crystallographica. Section F, Structural biology communications 20141031 Pt 11

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 acc  ...[more]

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