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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?
Author(s) -
Pintar Alessandro,
Guez Valerie,
Castagné Claire,
Bedouelle Hugues,
Delepierre Muriel
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00191-x
Subject(s) - transfer rna , linker , protein secondary structure , binding domain , c terminus , enzyme , biology , biochemistry , tyrosine , rna , stereochemistry , crystallography , binding site , chemistry , amino acid , gene , computer science , operating system
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.