1B8E

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

1B8E の概要

• エントリーDOI: 10.2210/pdb1b8e/pdb
• 分子名称: PROTEIN (BETA-LACTOGLOBULIN) (2 entities in total)
• 機能のキーワード: beta-lactoglobulin, variants, lipocalin, transport protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18301.17

構造登録者

Oliveira, K.M.G.,Sawyer, L.,Polikarpov, I. (登録日: 1999-01-30, 公開日: 2001-05-02, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.95 Å)