Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain?
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.
Pintar
A
A
Nuclear Magnetic Resonance Laboratory, Pasteur Institute, Paris, France.
Guez
V
V
Castagné
C
C
Bedouelle
H
H
Delepierre
M
M
D000595:Amino Acid Sequence; D000926:Anticodon; D001411:Geobacillus stearothermophilus / Q000737:chemistry / Q000201:enzymology*; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism
D000926:Anticodon; D014448:Tyrosine-tRNA Ligase