1AB1

SI FORM CRAMBIN

1AB1 の概要

• エントリーDOI: 10.2210/pdb1ab1/pdb
• 分子名称: CRAMBIN (SER22/ILE25), ETHANOL (2 entities in total)
• 機能のキーワード: thionin, plant seed protein
• 由来する生物種: Crambe hispanica subsp. abyssinica
• 細胞内の位置: Secreted: P01542
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4774.48

構造登録者

Teeter, M.M.,Yamano, A. (登録日: 1997-01-31, 公開日: 1997-08-12, 最終更新日: 2024-11-20)

主引用文献

Yamano, A.,Heo, N.H.,Teeter, M.M.
Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations.
J.Biol.Chem., 272:9597-9600, 1997

PubMed Abstract: It is not agreed that correlated positions of disordered protein side chains (substate correlations) can be deduced from diffraction data. The pure Ser-22/Ile-25 (SI form) crambin crystal structure confirms correlations deduced for the natural, mixed sequence form of crambin crystals. Physical separation of the mixed form into pure SI form and Pro-22/Leu-25 (PL form) crambin and the PL form crystal structure determination (Yamano, A., and Teeter, M. M. (1994) J. Biol. Chem. 269, 13956-13965) support the proposed (Teeter, M. M., Roe, S. M., and Heo, N. H. (1993) J. Mol. Biol. 230, 292-311) correlation model. Electron density of mixed form crambin crystals shows four possible pairs of side chain conformations for heterogeneous residue 22 and nearby Tyr-29 (2(2) = 4, two conformations for each of two side chains). One combination can be eliminated because of short van der Waals' contacts. However, only two alternates have been postulated to exist in mixed form crambin: Pro-22/Tyr-29A and Ser-22/Tyr-29B. In crystals of the PL form, Pro-22 and Tyr-29A are found to be in direct van der Waals' contact (Yamano, A., and Teeter, M. M. (1994) J. Biol. Chem. 269, 13956-13965). Comparison of the SI form structure with the mixed form electron density confirms that the fourth combination of side chains does not occur and that side chain correlations are mediated by water networks.

PubMed: 9092482
DOI: 10.1074/jbc.272.15.9597

実験手法

X-RAY DIFFRACTION (0.89 Å)