6GEL
The structure of TWITCH-2B
Summary for 6GEL
| Entry DOI | 10.2210/pdb6gel/pdb |
| Descriptor | Green fluorescent protein,Optimized Ratiometric Calcium Sensor,Green fluorescent protein,Green fluorescent protein, CALCIUM ION, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | fluorescent protein, twitch-2b, fret, ratiometric biosensor |
| Biological source | Aequorea victoria (Jellyfish) More |
| Total number of polymer chains | 2 |
| Total formula weight | 125954.95 |
| Authors | Trigo Mourino, P.,Paulat, M.,Thestrup, T.,Griesbeck, O.,Griesinger, C.,Becker, S. (deposition date: 2018-04-26, release date: 2019-08-21, Last modification date: 2024-11-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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