2WSO

Structure of Cerulean Fluorescent Protein at physiological pH

2WSO の概要

• エントリーDOI: 10.2210/pdb2wso/pdb
• 関連するPDBエントリー: 1B9C 1BFP 1C4F 1CV7 1EMA 1EMB 1EMC 1EME 1EMF 1EMG 1EMK 1EML 1EMM 1F09 1F0B 1GFL 1H6R 1HCJ 1HUY 1JBY 1JBZ 1JC0 1JC1 1KP5 1KYP 1KYR 1KYS 1MYW 1Q4A 1Q4B 1Q4C 1Q4D 1Q4E 1Q73 1QXT 1QY3 1QYF 1QYO 1QYQ 1RM9 1RMM 1RMO 1RMP 1RRX 1W7S 1W7T 1W7U 1YFP 1YHG 1YHH 1YHI 1YJ2 1YJF 1Z1P 1Z1Q 2AH8 2AHA 2B3P 2B3Q 2EMD 2EMN 2EMO 2FWQ 2FZU 2WSN 2YFP
• 分子名称: GREEN FLUORESCENT PROTEIN (2 entities in total)
• 機能のキーワード: fluorescent protein, chromophore, luminescence, photoprotein
• 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: 26789.24

構造登録者

Lelimousin, M.,Noirclerc-Savoye, M.,Lazareno-Saez, C.,Paetzold, B.,Le Vot, S.,Chazal, R.,Macheboeuf, P.,Field, M.J.,Bourgeois, D.,Royant, A. (登録日: 2009-09-08, 公開日: 2009-09-29, 最終更新日: 2024-10-23)

主引用文献

Lelimousin, M.,Noirclerc-Savoye, M.,Lazareno-Saez, C.,Paetzold, B.,Le Vot, S.,Chazal, R.,Macheboeuf, P.,Field, M.J.,Bourgeois, D.,Royant, A.
Intrinsic Dynamics in Ecfp and Cerulean Control Fluorescence Quantum Yield.
Biochemistry, 48:10038-, 2009

PubMed Abstract: Enhanced cyan fluorescent protein (ECFP) and its variant Cerulean are genetically encoded fluorophores widely used as donors in FRET-based cell imaging experiments. First, we have confirmed through denaturation experiments that the double-peak spectroscopic signature of these fluorescent proteins originates from the indole ring of the chromophore. Then, to explain the improvement in the fluorescence properties of Cerulean compared to those of ECFP, we have determined the high-resolution crystal structures of these two proteins at physiological pH and performed molecular dynamics simulations. In both proteins, the N-terminal half of the seventh strand exhibits two conformations. These conformations both have a complex set of van der Waals interactions with the chromophore and, as our simulations suggest, they interconvert on a nanosecond time scale. The Y145A and H148D mutations in Cerulean stabilize these interactions and allow the chromophore to be more planar, better packed, and less prone to collisional quenching, albeit only intermittently. As a consequence, the probability of nonradiative decay is significantly decreased. Our results highlight the considerable dynamical flexibility that exists in the vicinity of the tryptophan-based chromophore of these engineered fluorescent proteins and provide insights that should allow the design of mutants with enhanced optical properties.

PubMed: 19754158
DOI: 10.1021/BI901093W

実験手法

X-RAY DIFFRACTION (1.15 Å)