1h3e

From Proteopedia

Revision as of 13:22, 30 October 2007

TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL

Overview

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 ... [(full description)]

About this Structure

1H3E is a [Protein complex] structure of sequences from [Thermus thermophilus] with ATP and TYB as [ligands]. Active as [Tyrosine--tRNA ligase], with EC number [6.1.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

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: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]

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