1SRY

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

1SRY の概要

• エントリーDOI: 10.2210/pdb1sry/pdb
• 分子名称: SERYL-tRNA SYNTHETASE (2 entities in total)
• 機能のキーワード: ligase(synthetase)
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm (By similarity): P34945
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95757.66

構造登録者

Fujinaga, M.,Berthet-Colominas, C.,Cusack, S. (登録日: 1993-08-10, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)