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

Мова статті: 
Англійська
Автор(и) статті: 
Pydiura N.A., Kornelyuk A.I.
Вихідні данні статті: 
Biopolymers and Cell, 28, N5, 397-403 (2012)
Назва журналу: 
Biopolymers and Cell
Рік публікації: 
2012
Volume: 
28
Issue: 
5
Ключові слова: 
tyrosyl-tRNA synthetase, homology modeling, interdomain linker, c-Abl tyrosine kinase, EMAP II, tRNA Tyr
Ключове слово: 
tyrosyl-trna synthetase
Ключове слово: 
homology modeling
Ключове слово: 
interdomain linker
Ключове слово: 
c-abl tyrosine kinase
Ключове слово: 
emap ii
Ключове слово: 
trna tyr

Mammalian tyrosyl-tRNA synthetase is composed of two structural modules: N-terminal catalytic miniTyrRS and
non-catalytic cytokine-like C-terminal module connected bya flexible peptide linker. Till now, the 3D structure
of any full-length mammalian TyrRS has not been solved by X-ray crystallography. Theaimof this work was a ho-mology modeling of 3D structure of full-lehgth B.taurus tyrosyl-tRNA synthetase.Methods. Homology modeling
of TyrRS was performed by Modeller 9.1 package. Quality of the models was assessed using Biotech Validation
Suite web-server.Results. Our BLAST search identified 34% sequence homology between interdomain linker of
TyrRS and linker of human c-Abl tyrosine kinase. In order to model the full-length TyrRS structure we as-sembled the models of three parts of the protein (N- and C- terminal domains and the linker) using Modeller 9.1
software. The best Abl-17 model structure was refined by energy minimization.Conclusions. High flexibility of
the interdomain linker can generate multiple conformations of TyrRS. The hinge mechanism at interdomain
linker may be provided by conservative Gly353. It is proposed, that due to the linker flexibility an open extended
conformation of TyrRS could transform into closedconformations in the enzyme-substrate complexes.

Назва підрозділу: 
Кафедра молекулярної біології, біотехнології та біофізики
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Дизайн: Інститут високих технологій
Ivan Ivanov