1h3f
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TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TYROSINOL
OverviewOverview
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.
About this StructureAbout this Structure
1H3F is a Single protein structure of sequence from Thermus thermophilus with SO4 and TYB as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:12110594 [[Category: atp + l-tyrosine + trna(tyr)->amp + ppi + l-tyrosyl-trna(ty class i aminoacyl-trna synthetase]]
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