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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
It has been recently shown that orthogonal tRNA/aminoacyl-tRNA synthetase pairs can be evolved to allow genetic incorporation of unnatural amino acids into proteins in both prokaryotes and eukaryotes. Here we describe the crystal structure of an evolved aminoacyl-tRNA synthetase that charges the unnatural amino acid p-acetylphenylalanine. Molecular recognition is due to altered hydrogen bonding and packing interactions with bound substrate that result from changes in both side-chain and backbone conformation.
Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase.,Turner JM, Graziano J, Spraggon G, Schultz PG J Am Chem Soc. 2005 Nov 2;127(43):14976-7. PMID:16248607[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Turner JM, Graziano J, Spraggon G, Schultz PG. Structural characterization of a p-acetylphenylalanyl aminoacyl-tRNA synthetase. J Am Chem Soc. 2005 Nov 2;127(43):14976-7. PMID:16248607 doi:10.1021/ja0549042
