2QJ7

PYP ultra-high resolution of a bacterial photoreceptor

2QJ7 の概要

• エントリーDOI: 10.2210/pdb2qj7/pdb
• 関連するPDBエントリー: 2QJ5
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: pyp, pas domain, signal transduction, signaling protein
• 由来する生物種: Halorhodospira halophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.73

構造登録者

Coureux, P.D.,Fan, Z.P.,Stojanoff, V.,Genick, U.K. (登録日: 2007-07-06, 公開日: 2008-05-20, 最終更新日: 2023-08-30)

主引用文献

Coureux, P.D.,Fan, Z.P.,Stojanoff, V.,Genick, U.K.
Picometer-scale conformational heterogeneity separates functional from nonfunctional States of a photoreceptor protein.
Structure, 16:863-872, 2008

PubMed Abstract: Protein structural fluctuations occur over a wide spatial scale, ranging from minute, picometer-scale displacements, to large, interdomain motions and partial unfolding. While large-scale protein structural changes and their effects on protein function have been the focus of much recent attention, small-scale fluctuations have been less well studied, and are generally assumed to have proportionally smaller effects. Here we use the bacterial photoreceptor photoactive yellow protein (PYP) to test if subtle structural changes do, indeed, imply equally subtle functional effects. We flash froze crystals of PYP to trap the protein's conformational ensemble, and probed the molecules in this ensemble for their ability to facilitate PYP's biological function (i.e., light-driven isomerization of its chromophore). Our results indicate that the apparently homogeneous structural state observed in a 0.82 A crystal structure in fact comprises an ensemble of conformational states, in which subpopulations with nearly identical structures display dramatically different functional properties.

PubMed: 18547519
DOI: 10.1016/j.str.2008.02.022

実験手法

X-RAY DIFFRACTION (1.05 Å)