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

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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 α+β 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.