 |
Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-00370448
Contributor : Cécile Roux Connect in order to contact the contributor
Submitted on : Tuesday, March 24, 2009 - 2:05:23 PM
Last modification on : Tuesday, October 19, 2021 - 10:27:24 PM
Contributor : Cécile Roux Connect in order to contact the contributor
Submitted on : Tuesday, March 24, 2009 - 2:05:23 PM
Last modification on : Tuesday, October 19, 2021 - 10:27:24 PM
Links full text
