Flexible 3D structure of Bos taurus tyrosyl-tRNA synthetase suggests the existence of the hinge mechanism provided by conservative Gly353 at interdomain linker

• Published in: Вiopolymers and Cell
• Date: 2012
• Main Authors: Pydiura, N.A., Kornelyuk, A.I.
• Format: Article
• Language: English
• Published: Інститут молекулярної біології і генетики НАН України 2012
• Subjects: Bioinformatics
• Online Access: https://nasplib.isofts.kiev.ua/handle/123456789/156942
• Journal Title: Digital Library of Periodicals of National Academy of Sciences of Ukraine
• Cite this: Flexible 3D structure of Bos taurus tyrosyl-tRNA
 synthetase suggests the existence of the hinge mechanism
 provided by conservative Gly353 at interdomain linker / N.A. Pydiura, A.I. Kornelyuk // Вiopolymers and Cell. — 2012. — Т. 28, № 5. — С. 397-403. — Бібліогр.: 35 назв. — англ.

Mammalian tyrosyl-tRNA synthetase is composed of two structural modules: N-terminal catalytic miniTyrRS and non-catalytic cytokine-like C-terminal module connected by a flexible peptide linker. Till now, the 3D structure of any full-length mammalian TyrRS has not been solved by X-ray crystallography...