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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. |
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| Authors: | Clara Smal Serena Zanzoni Mariapina D’Onofrio Henriette Molinari Daniel O. Cicero Michael Assfalg |
| Affiliation: | 1. Fundación Instituto Leloir, Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina 2. Dipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, 37134, Verona, Italy 3. CNR-ISMAC, Via Bassini 15, 20133, Milan, Italy 4. Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma “Tor Vergata”, Via della Ricerca Scientifica SNC, 00133, Rome, Italy |
| 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. |
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