title: ¹H, ¹⁵N, and ¹³C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.
abstract: 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.
authors.affiliation: Fundación Instituto Leloir, Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina.
authors.forename: Clara
authors.initials: C
authors.lastname: Smal
authors.forename: Serena
authors.initials: S
authors.lastname: Zanzoni
authors.forename: Mariapina
authors.initials: M
authors.lastname: D'Onofrio
authors.forename: Henriette
authors.initials: H
authors.lastname: Molinari
authors.forename: Daniel O
authors.initials: DO
authors.lastname: Cicero
authors.forename: Michael
authors.initials: M
authors.lastname: Assfalg
mesh_terms: D000412:Alanine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism; D041965:Flavobacteriaceae / Q000201:enzymology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000378:metabolism
chemical_list: D012343:RNA, Transfer; D000412:Alanine-tRNA Ligase