3N2Y

Crystal structure of tyrosyl-tRNA synthetase complexed with p-(2-tetrazolyl)-phenylalanine

Summary for 3N2Y

• Entry DOI: 10.2210/pdb3n2y/pdb
• Descriptor: Tyrosyl-tRNA synthetase, 4-(2H-tetrazol-2-yl)-L-phenylalanine (3 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, photoclick chemistry, p-(2-tetrazolyl)-phenylalanine, ligase
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Cellular location: Cytoplasm: Q57834
• Total number of polymer chains: 2
• Total formula weight: 72492.19

Authors

Wu, M.,Li, J.,Zang, J. (deposition date: 2010-05-19, release date: 2010-11-03, Last modification date: 2023-11-01)

Primary citation

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., 132:14812-14818, 2010

PubMed Abstract: 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.

PubMed: 20919707
DOI: 10.1021/ja104350y

Experimental method

X-RAY DIFFRACTION (2.49 Å)