1JXT

CRAMBIN MIXED SEQUENCE FORM AT 160 K. PROTEIN/WATER SUBSTATES

1JXT の概要

• エントリーDOI: 10.2210/pdb1jxt/pdb
• 関連するPDBエントリー: 1JXU 1JXW 1JXX 1JXY 1ab1 1cbn 1cnr 1crn
• 分子名称: Crambin, ETHANOL (2 entities in total)
• 機能のキーワード: water, substate, function, plant 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.,Stec, B.,Mohanty, U. (登録日: 2001-09-08, 公開日: 2001-10-31, 最終更新日: 2024-10-30)

主引用文献

Teeter, M.M.,Yamano, A.,Stec, B.,Mohanty, U.
On the nature of a glassy state of matter in a hydrated protein: Relation to protein function.
Proc.Natl.Acad.Sci.USA, 98:11242-11247, 2001

PubMed Abstract: Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.

PubMed: 11572978
DOI: 10.1073/pnas.201404398

実験手法

X-RAY DIFFRACTION (0.89 Å)