6WN2

Tyrosyl t-RNA Synthetase Mutant from E.coli Complexed with sulfotyrosine

Summary for 6WN2

• Entry DOI: 10.2210/pdb6wn2/pdb
• Descriptor: Tyrosine--tRNA ligase, O-SULFO-L-TYROSINE, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: tyrrs, sulfotyrosine, ligase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 74183.39

Authors

Beltran, D.G.,Zhang, L. (deposition date: 2020-04-22, release date: 2020-09-02, Last modification date: 2024-03-06)

Primary citation

He, X.,Chen, Y.,Beltran, D.G.,Kelly, M.,Ma, B.,Lawrie, J.,Wang, F.,Dodds, E.,Zhang, L.,Guo, J.,Niu, W.
Functional genetic encoding of sulfotyrosine in mammalian cells.
Nat Commun, 11:4820-4820, 2020

PubMed Abstract: Protein tyrosine O-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.

PubMed: 32973160
DOI: 10.1038/s41467-020-18629-9

Experimental method

X-RAY DIFFRACTION (1.78 Å)