6GEL
The structure of TWITCH-2B
6GEL の概要
| エントリーDOI | 10.2210/pdb6gel/pdb |
| 分子名称 | Green fluorescent protein,Optimized Ratiometric Calcium Sensor,Green fluorescent protein,Green fluorescent protein, CALCIUM ION, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | fluorescent protein, twitch-2b, fret, ratiometric biosensor |
| 由来する生物種 | Aequorea victoria (Jellyfish) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 125954.95 |
| 構造登録者 | Trigo Mourino, P.,Paulat, M.,Thestrup, T.,Griesbeck, O.,Griesinger, C.,Becker, S. (登録日: 2018-04-26, 公開日: 2019-08-21, 最終更新日: 2024-11-20) |
| 主引用文献 | Trigo-Mourino, P.,Thestrup, T.,Griesbeck, O.,Griesinger, C.,Becker, S. Dynamic tuning of FRET in a green fluorescent protein biosensor. Sci Adv, 5:eaaw4988-eaaw4988, 2019 Cited by PubMed Abstract: Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with -dependent paramagnetic nuclear magnetic resonance at 900 MHz and 1.1 GHz. These structural data provide the unprecedented opportunity to calculate FRET from the x-ray structure and to compare it to experimental data in solution. We find that interdomain dynamics limits the FRET effect and show that a rigidification of the sensor further enhances FRET. PubMed: 31457088DOI: 10.1126/sciadv.aaw4988 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.51 Å) |
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