3TEH

Crystal structure of Thermus thermophilus Phenylalanyl-tRNA synthetase complexed with L-dopa

Summary for 3TEH

• Entry DOI: 10.2210/pdb3teh/pdb
• Related: 3HFZ 3TEG
• Descriptor: Phenylalanyl-tRNA synthetase alpha chain, Phenylalanyl-tRNA synthetase beta chain, 3,4-DIHYDROXYPHENYLALANINE, ... (4 entities in total)
• Functional Keywords: aars, l-dopa, trna, ligase
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P27001 P27002
• Total number of polymer chains: 2
• Total formula weight: 126424.23

Authors

Safro, M.,Klipcan, L.,Moor, N. (deposition date: 2011-08-14, release date: 2011-11-23, Last modification date: 2024-02-28)

Primary citation

Moor, N.,Klipcan, L.,Safro, M.G.
Bacterial and Eukaryotic Phenylalanyl-tRNA Synthetases Catalyze Misaminoacylation of tRNA(Phe) with 3,4-Dihydroxy-L-Phenylalanine.
Chem.Biol., 18:1221-1229, 2011

PubMed Abstract: Aminoacyl-tRNA synthetases exert control over the accuracy of translation by selective pairing the correct amino acids with their cognate tRNAs, and proofreading the misacylated products. Here we show that three existing, structurally different phenylalanyl-tRNA synthetases-human mitochondrial (HsmtPheRS), human cytoplasmic (HsctPheRS), and eubacterial from Thermus thermophilus (TtPheRS), catalyze mischarging of tRNA(Phe) with an oxidized analog of tyrosine-L-dopa. The lowest level of L-dopa discrimination over the cognate amino acid, exhibited by HsmtPheRS, is comparable to that of tyrosyl-tRNA synthetase. HsmtPheRS and TtPheRS complexes with L-dopa revealed in the active sites an electron density shaping this ligand. HsctPheRS and TtPheRS possessing editing activity are capable of hydrolyzing the exogenous L-dopa-tRNA(Phe) as efficiently as Tyr-tRNA(Phe). However, editing activity of PheRS does not guarantee reduction of the aminoacylation error rate to escape misincorporation of L-dopa into polypeptide chains.

PubMed: 22035791
DOI: 10.1016/j.chembiol.2011.08.008

Experimental method

X-RAY DIFFRACTION (2.8524 Å)