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

Alessandro Pintar (1) , Valérie Guez (2) , Claire Castagné (1) , Hugues Bedouelle (2) , Muriel Delepierre (1)

1 Résonance Magnétique Nucléaire
2 Biochimie cellulaire

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.

Domains: Structural Biology [q-bio.BM]

Alessandro Pintar, Valérie Guez, Claire Castagné, Hugues Bedouelle, Muriel Delepierre. Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain?. FEBS Letters, 1999, 446 (1), pp.81-5. ⟨10.1016/S0014-5793(99)00191-X⟩. ⟨pasteur-00370448⟩