4RVZ

Crystal structure of tRNA fluorescent labeling enzyme

Summary for 4RVZ

• Entry DOI: 10.2210/pdb4rvz/pdb
• Descriptor: tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS, ZINC ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: trna modification, phosphorylation, tias, ligase
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cytoplasm : O28025
• Total number of polymer chains: 1
• Total formula weight: 49162.86

Authors

Dong, J.,Li, F.,Wang, J.,Gong, W. (deposition date: 2014-11-29, release date: 2015-03-11, Last modification date: 2024-11-27)

Primary citation

Li, F.,Dong, J.,Hu, X.,Gong, W.,Li, J.,Shen, J.,Tian, H.,Wang, J.
A covalent approach for site-specific RNA labeling in Mammalian cells.
Angew.Chem.Int.Ed.Engl., 54:4597-4602, 2015

PubMed Abstract: Advances in RNA research and RNA nanotechnology depend on the ability to manipulate and probe RNA with high precision through chemical approaches, both in vitro and in mammalian cells. However, covalent RNA labeling methods with scope and versatility comparable to those of current protein labeling strategies are underdeveloped. A method is reported for the site- and sequence-specific covalent labeling of RNAs in mammalian cells by using tRNA(Ile2) -agmatidine synthetase (Tias) and click chemistry. The crystal structure of Tias in complex with an azide-bearing agmatine analogue was solved to unravel the structural basis for Tias/substrate recognition. The unique RNA sequence specificity and plastic Tias/substrate recognition enable the site-specific transfer of azide/alkyne groups to an RNA molecule of interest in vitro and in mammalian cells. Subsequent click chemistry reactions facilitate the versatile labeling, functionalization, and visualization of target RNA.

PubMed: 25694369
DOI: 10.1002/anie.201410433

Experimental method

X-RAY DIFFRACTION (2.9 Å)