1B8E

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP

Summary for 1B8E

• Entry DOI: 10.2210/pdb1b8e/pdb
• Descriptor: PROTEIN (BETA-LACTOGLOBULIN) (2 entities in total)
• Functional Keywords: beta-lactoglobulin, variants, lipocalin, transport protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 18301.17

Authors

Oliveira, K.M.G.,Sawyer, L.,Polikarpov, I. (deposition date: 1999-01-30, release date: 2001-05-02, Last modification date: 2024-11-20)

Primary citation

Oliveira, K.M.,Valente-Mesquita, V.L.,Botelho, M.M.,Sawyer, L.,Ferreira, S.T.,Polikarpov, I.
Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition.
Eur.J.Biochem., 268:477-483, 2001

PubMed Abstract: The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit the open conformation of the EF loop at the pH of crystallization (pH 7.9), in contrast to what has been reported for the same genetic variants at pH 7.1 in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. & Jameson, G.B. (1999) Protein Sci. 8, 75-83]. Furthermore, it was found that the stereochemical environment of Tyr42 changes significantly with pH variation between pH 7 and pH 8. This may provide a structural explanation for an as yet unexplained feature of the Tanford transition, namely the increase in exposure of a tyrosine residue.

PubMed: 11168385

Experimental method

X-RAY DIFFRACTION (1.95 Å)