1BSY

STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1

1BSY の概要

• エントリーDOI: 10.2210/pdb1bsy/pdb
• 分子名称: BETA-LACTOGLOBULIN (2 entities in total)
• 機能のキーワード: transport, beta-lactoglobulin, ph-dependent conformation, loop movement, tanford transition
• 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: 18387.26

構造登録者

Qin, B.Y.,Bewley, M.C.,Creamer, L.K.,Baker, E.N.,Jameson, G.B. (登録日: 1998-08-31, 公開日: 1999-01-27, 最終更新日: 2011-07-13)

主引用文献

Qin, B.Y.,Bewley, M.C.,Creamer, L.K.,Baker, H.M.,Baker, E.N.,Jameson, G.B.
Structural basis of the Tanford transition of bovine beta-lactoglobulin.
Biochemistry, 37:14014-14023, 1998

PubMed Abstract: The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.

PubMed: 9760236
DOI: 10.1021/bi981016t

実験手法

X-RAY DIFFRACTION (2.24 Å)