1sry

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Image:1sry.gif

1sry, resolution 2.5Å

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REFINED CRYSTAL STRUCTURE OF THE SERYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION

Overview

The three-dimensional structure of the seryl-tRNA synthetase from Thermus thermophilus has been determined and refined at 2.5 A resolution. The final model consists of a dimer of 421 residues each and 190 water molecules. The R-factor is 18.4% for all the data between 10 and 2.5 A resolution. The structure is very similar to that of the homologous enzyme from Escherichia coli, with an r.m.s. difference of 1.5 A for the 357 alpha-carbon atoms considered equivalent. The comparison of the two structures indicates increased hydrophobicity, reduced conformational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile.

About this Structure

1SRY is a Single protein structure of sequence from Thermus thermophilus. Active as Serine--tRNA ligase, with EC number 6.1.1.11 Full crystallographic information is available from OCA.

Reference

Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution., Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S, J Mol Biol. 1993 Nov 5;234(1):222-33. PMID:8230201

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