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© Research
Publication : FEBS letters

Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain?

Team: Archived: Nuclear Magnetic Resonance Of Biomolecules
Member: Muriel Delepierre
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 01 Mar 1999

Pintar A, Guez V, Castagné C, Bedouelle H, Delepierre M

Link to Pubmed [PMID] – 10100619

FEBS Lett. 1999 Mar;446(1):81-5

The tyrosyl-tRNA synthetase catalyzes the activation of tyrosine and its coupling to the cognate tRNA. The enzyme is made of two domains: an N-terminal catalytic domain and a C-terminal domain that is necessary for tRNA binding and for which it was not possible to determine the structure by X-ray crystallography. We determined the secondary structure of the C-terminal domain of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus by nuclear magnetic resonance methods and found that it is of the alpha+beta type. Its arrangement differs from those of the other anticodon binding domains whose structure is known. We also found that the isolated C-terminal domain behaves as a folded globular protein, and we suggest the presence of a flexible linker between the two domains.

http://www.ncbi.nlm.nih.gov/pubmed/10100619