7ZBA
HaloTag with Me-TRaQ-G ligand
Summary for 7ZBA
| Entry DOI | 10.2210/pdb7zba/pdb |
| Descriptor | Haloalkane dehalogenase, GLYCEROL, 4-(7-azanyl-5,5-dimethyl-3-methylimino-benzo[b][1]benzosilin-10-yl)-N-[2-[2-(6-chloranylhexoxy)ethoxy]ethyl]-3-methyl-benzamide, ... (5 entities in total) |
| Functional Keywords | halotag, haloalkane dehalogenase, silicon rhodamine, hydrolase |
| Biological source | Rhodococcus sp. |
| Total number of polymer chains | 2 |
| Total formula weight | 71058.92 |
| Authors | Emmert, S.,Rivera-Fuentes, P.,Pojer, F.,Lau, K. (deposition date: 2022-03-23, release date: 2023-02-01, Last modification date: 2024-10-23) |
| Primary citation | Emmert, S.,Quargnali, G.,Thallmair, S.,Rivera-Fuentes, P. A locally activatable sensor for robust quantification of organellar glutathione. Nat.Chem., 15:1415-1421, 2023 Cited by PubMed Abstract: Glutathione (GSH) is the main determinant of intracellular redox potential and participates in multiple cellular signalling pathways. Achieving a detailed understanding of intracellular GSH homeostasis depends on the development of tools to map GSH compartmentalization and intra-organelle fluctuations. Here we present a GSH-sensing platform for live-cell imaging, termed targetable ratiometric quantitative GSH (TRaQ-G). This chemogenetic sensor possesses a unique reactivity turn-on mechanism, ensuring that the small molecule is only sensitive to GSH in a desired location. Furthermore, TRaQ-G can be fused to a fluorescent protein to give a ratiometric response. Using TRaQ-G fused to a redox-insensitive fluorescent protein, we demonstrate that the nuclear and cytosolic GSH pools are independently regulated during cell proliferation. This sensor was used in combination with a redox-sensitive fluorescent protein to quantify redox potential and GSH concentration simultaneously in the endoplasmic reticulum. Finally, by exchanging the fluorescent protein, we created a near-infrared, targetable and quantitative GSH sensor. PubMed: 37322101DOI: 10.1038/s41557-023-01249-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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