1ati

From Proteopedia

Revision as of 13:45, 5 November 2007

CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Overview

The sequence and crystal structure at 2.75 A resolution of the homodimeric, glycyl-tRNA synthetase from Thermus thermophilus, the first representative, of the last unknown class II synthetase subgroup, have been determined., The three class II synthetase sequence motifs are present but the, structure was essential for identification of motif 1, which does not, possess the proline previously believed to be an essential class II, invariant. Nevertheless, crucial contacts with the active site of the, other monomer involving motif 1 are conserved and a more comprehensive, description of class II now becomes possible. Each monomer consists of an, active site strongly resembling that of the aspartyl and seryl enzymes, a, C-terminal anticodon recognition domain of 100 residues and a third domain, unusually inserted between motifs 1 and 2 almost certainly interacting, with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel, five-stranded parallel-antiparallel beta-sheet structure with three, surrounding helices. The active site residues most probably responsible, for substrate recognition, in particular in the Gly binding pocket, can be, identified by inference from aspartyl-tRNA synthetase due to the conserved, nature of the class II active site.

About this Structure

1ATI is a Single protein structure of sequence from Thermus thermophilus. Active as Glycine--tRNA ligase, with EC number 6.1.1.14 Structure known Active Site: SA1. Full crystallographic information is available from OCA.

Reference

Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:7556056

Page seeded by OCA on Mon Nov 5 15:51:06 2007