1ATI

CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Summary for 1ATI

• Entry DOI: 10.2210/pdb1ati/pdb
• Descriptor: GLYCYL-TRNA SYNTHETASE, GLYCYL-tRNA SYNTHETASE, ... (4 entities in total)
• Functional Keywords: protein biosynthesis, ligase, synthetase, aminoacyl-trna synthetase
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P56206
• Total number of polymer chains: 4
• Total formula weight: 120874.53

Authors

Logan, D.T.,Mazauric, M.-H.,Kern, D.,Moras, D. (deposition date: 1996-04-23, release date: 1997-07-07, Last modification date: 2024-02-07)

Primary citation

Logan, D.T.,Mazauric, M.H.,Kern, D.,Moras, D.
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.
EMBO J., 14:4156-4167, 1995

PubMed Abstract: 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.

PubMed: 7556056

Experimental method

X-RAY DIFFRACTION (2.75 Å)