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| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools > print |
| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools > print |
| 001 | 842277 | ||
| 005 | 20220930130139.0 | ||
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| 100 | 1 | _ | |0 P:(DE-Juel1)161543 |a Arinkin, Vladimir |b 0 |
| 245 | _ | _ | |a Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools |
| 260 | _ | _ | |a London |b Nature Publishing Group |c 2017 |
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| 520 | _ | _ | |a Unique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12–19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 Å resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Fα helix, shortening of the Eα-Fα loop and partial unfolding of the Eα helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies. |
| 536 | _ | _ | |0 G:(DE-HGF)POF3-581 |a 581 - Biotechnology (POF3-581) |c POF3-581 |f POF III |x 0 |
| 536 | _ | _ | |0 G:(DE-HGF)POF3-551 |a 551 - Functional Macromolecules and Complexes (POF3-551) |c POF3-551 |f POF III |x 1 |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 700 | 1 | _ | |0 P:(DE-Juel1)131965 |a Granzin, Joachim |b 1 |
| 700 | 1 | _ | |0 P:(DE-Juel1)157880 |a Röllen, Katrin |b 2 |
| 700 | 1 | _ | |0 P:(DE-Juel1)131482 |a Krauss, Ulrich |b 3 |
| 700 | 1 | _ | |0 P:(DE-Juel1)131457 |a Jaeger, Karl-Erich |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, Dieter |b 5 |
| 700 | 1 | _ | |0 P:(DE-Juel1)131950 |a Batra-Safferling, Renu |b 6 |e Corresponding author |
| 773 | _ | _ | |0 PERI:(DE-600)2615211-3 |a 10.1038/srep42971 |g Vol. 7, p. 42971 - |p 42971 - |t Scientific reports |v 7 |x 2045-2322 |y 2017 |
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