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

Abstract : 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.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-00370448
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Submitted on : Tuesday, March 24, 2009 - 2:05:23 PM
Last modification on : Monday, January 13, 2020 - 5:08:14 PM

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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, Wiley, 1999, 446 (1), pp.81-5. ⟨10.1016/S0014-5793(99)00191-X⟩. ⟨pasteur-00370448⟩

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