| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The MetRS-N domain binds an Arc1-P domain in a tetrameric complex resembling a classical GST homo-dimer. Domain-swapping between symmetrically related MetRS-N and Arc1p-N domains generates a 2:2 tetramer held together by van der Waals forces. This domain is necessary for formation of the aminoacyl-tRNA synthetase complex necessary for tRNA nuclear export and shuttling as part of the translational apparatus. The domain is associated with PF09334.
This entry represents the N-terminal domain of methionyl-tRNA synthetase (MetRS). This N-terminal appended domain mediates non-catalytic complex formation through its interaction with a domain in the tRNA aminoacylation cofactor Arc1p. The interacting domains of MetRS, GluRS (glutamyl-tRNA synthetase) and Arc1p form a ternary complex resembling a classical GST homo-dimer [PUBMED:16914447]. Domain-swapping between symmetrically related MetRS-N and Arc1p-N domains generates a 2:2 tetramer held together by van der Waals forces. This domain is necessary for formation of the aminoacyl-tRNA synthetase complex necessary for tRNA nuclear export and shuttling as part of the translational apparatus.
Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D; , Nucleic Acids Res. 2006;34:3968-3979.: Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. PUBMED:16914447 EPMC:16914447.
