7ZIZ
X-ray structure of the dead variant haloalkane dehalogenase HaloTag7-D106A bound to a pentanol tetramethylrhodamine ligand (TMR-Hy5)
Summary for 7ZIZ
| Entry DOI | 10.2210/pdb7ziz/pdb |
| Related | 7ZIV 7ZIW 7ZIX 7ZIY 7ZJ0 |
| Descriptor | Haloalkane dehalogenase, [9-[2-carboxy-5-[2-[2-(5-oxidanylpentoxy)ethoxy]ethylcarbamoyl]phenyl]-6-(dimethylamino)xanthen-3-ylidene]-dimethyl-azanium, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | haloalkane dehalogenase, halotag, halotag7, self-labeling protein, fluorophore, tetramethylrhodamine, hydrolase |
| Biological source | Rhodococcus sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 33914.23 |
| Authors | Tarnawski, M.,Kompa, J.,Johnsson, K.,Hiblot, J. (deposition date: 2022-04-08, release date: 2023-02-22, Last modification date: 2024-02-07) |
| Primary citation | Kompa, J.,Bruins, J.,Glogger, M.,Wilhelm, J.,Frei, M.S.,Tarnawski, M.,D'Este, E.,Heilemann, M.,Hiblot, J.,Johnsson, K. Exchangeable HaloTag Ligands for Super-Resolution Fluorescence Microscopy. J.Am.Chem.Soc., 145:3075-3083, 2023 Cited by PubMed Abstract: The specific and covalent labeling of the protein HaloTag with fluorescent probes in living cells makes it a powerful tool for bioimaging. However, the irreversible attachment of the probe to HaloTag precludes imaging applications that require transient binding of the probe and comes with the risk of irreversible photobleaching. Here, we introduce exchangeable ligands for fluorescence labeling of HaloTag (xHTLs) that reversibly bind to HaloTag and that can be coupled to rhodamines of different colors. In stimulated emission depletion (STED) microscopy, probe exchange of xHTLs allows imaging with reduced photobleaching as compared to covalent HaloTag labeling. Transient binding of fluorogenic xHTLs to HaloTag fusion proteins enables points accumulation for imaging in nanoscale topography (PAINT) and MINFLUX microscopy. We furthermore introduce pairs of xHTLs and HaloTag mutants for dual-color PAINT and STED microscopy. xHTLs thus open up new possibilities in imaging across microscopy platforms for a widely used labeling approach. PubMed: 36716211DOI: 10.1021/jacs.2c11969 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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