3DQK

Structure of the Yellow Fluorescent Protein Citrine Frozen at 1000 Atmospheres Number 2: Structure 6 in a Series of 26 High Pressure Structures

3DQK の概要

• エントリーDOI: 10.2210/pdb3dqk/pdb
• 関連するPDBエントリー: 1F09 1F0B 1HUY 1YFP 2YFP 3DPW 3DPX 3DPZ 3DQ1 3DQ2 3DQ3 3DQ4 3DQ5 3DQ6 3DQ7 3DQ8 3DQ9 3DQA 3DQC 3DQD 3DQE 3DQF 3DQH 3DQI 3DQJ 3DQL 3DQM 3DQN 3DQO 3DQU
• 分子名称: Green fluorescent protein (2 entities in total)
• 機能のキーワード: yellow fluorescent protein, beta barrel, chromophore, fluorescent protein, high pressure, luminescence, photoprotein, luminescent protein
• 由来する生物種: Aequorea victoria (Jellyfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27393.92

構造登録者

Barstow, B.,Kim, C.U. (登録日: 2008-07-09, 公開日: 2008-09-23, 最終更新日: 2023-11-15)

主引用文献

Barstow, B.,Ando, N.,Kim, C.U.,Gruner, S.M.
Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift.
Proc.Natl.Acad.Sci.Usa, 105:13362-13366, 2008

PubMed Abstract: A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 A at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.

PubMed: 18768811
DOI: 10.1073/pnas.0802252105

実験手法

X-RAY DIFFRACTION (1.4 Å)