Structural highlights
Function
[SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[1]
Publication Abstract from PubMed
Light-induced chemical reactions exist in nature, regulating many important cellular and organismal functions, e.g., photosensing in prokaryotes and vision formation in mammals. Here, we report the genetic incorporation of a photoreactive unnatural amino acid, p-(2-tetrazole)phenylalanine (p-Tpa), into myoglobin site-specifically in E. coli by evolving an orthogonal tRNA/aminoacyl-tRNA synthetase pair and the use of p-Tpa as a bioorthogonal chemical "handle" for fluorescent labeling of p-Tpa-encoded myoglobin via the photoclick reaction. Moreover, we elucidated the structural basis for the biosynthetic incorporation of p-Tpa into proteins by solving the X-ray structure of p-Tpa-specific aminoacyl-tRNA synthetase in complex with p-Tpa. The genetic encoding of this photoreactive amino acid should make it possible in the future to photoregulate protein function in living systems.
A biosynthetic route to photoclick chemistry on proteins.,Wang J, Zhang W, Song W, Wang Y, Yu Z, Li J, Wu M, Wang L, Zang J, Lin Q J Am Chem Soc. 2010 Oct 27;132(42):14812-8. PMID:20919707[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Steer BA, Schimmel P. Major anticodon-binding region missing from an archaebacterial tRNA synthetase. J Biol Chem. 1999 Dec 10;274(50):35601-6. PMID:10585437
- ↑ Wang J, Zhang W, Song W, Wang Y, Yu Z, Li J, Wu M, Wang L, Zang J, Lin Q. A biosynthetic route to photoclick chemistry on proteins. J Am Chem Soc. 2010 Oct 27;132(42):14812-8. PMID:20919707 doi:10.1021/ja104350y
