CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

File:1ati.gif


1ati, resolution 2.75Å

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OverviewOverview

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 ... [(full description)]

About this StructureAbout 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].

ReferenceReference

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

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