1H3E

Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA) and with ATP and tyrosinol

Summary for 1H3E

• Entry DOI: 10.2210/pdb1h3e/pdb
• Related: 1H3F
• Descriptor: TYROSYL-TRNA SYNTHETASE, WILD-TYPE TRNATYR(GUA), ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: ligase, class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)
• Biological source: THERMUS THERMOPHILUS; More
• Total number of polymer chains: 2
• Total formula weight: 77170.10

Authors

Cusack, S.,Yaremchuk, A.,Kriklivyi, I.,Tukalo, M. (deposition date: 2002-08-28, release date: 2002-10-27, Last modification date: 2024-05-01)

Primary citation

Yaremchuk, A.,Kriklivyi, I.,Tukalo, M.,Cusack, S.
Class I Tyrosyl-tRNA Synthetase Has a Class II Mode or tRNA Recognition
Embo J., 21:3829-, 2002

PubMed Abstract: Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem.

PubMed: 12110594
DOI: 10.1093/EMBOJ/CDF373

Experimental method

X-RAY DIFFRACTION (2.9 Å)