RESUMEN

A gene encoding a protein classified as alanyl-tRNA synthetase (AlaRS) was found in the genome of the psychrophilic bacteria Bizionia argentinensis. The enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Herein we report the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from B. argentinensis. The chemical shift data, reported for the first time for a C-Ala domain, constitute the basis for NMR structural studies aimed at elucidating the cold-adaptation mechanism of AlaRS.

Asunto(s)

Alanina-ARNt Ligasa/química , Flavobacteriaceae/enzimología , Resonancia Magnética Nuclear Biomolecular , Alanina-ARNt Ligasa/metabolismo , Estructura Terciaria de Proteína , ARN de Transferencia/metabolismo