1SRY

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

Summary for 1SRY

• Entry DOI: 10.2210/pdb1sry/pdb
• Descriptor: SERYL-tRNA SYNTHETASE (2 entities in total)
• Functional Keywords: ligase(synthetase)
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (By similarity): P34945
• Total number of polymer chains: 2
• Total formula weight: 95757.66

Authors

Fujinaga, M.,Berthet-Colominas, C.,Cusack, S. (deposition date: 1993-08-10, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Fujinaga, M.,Berthet-Colominas, C.,Yaremchuk, A.D.,Tukalo, M.A.,Cusack, S.
Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution.
J.Mol.Biol., 234:222-233, 1993

PubMed Abstract: 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.

PubMed: 8230201
DOI: 10.1006/jmbi.1993.1576

Experimental method

X-RAY DIFFRACTION (2.5 Å)