嗜冷细菌阿根廷比齐奥尼亚菌丙氨酰 - tRNA合成酶C - 丙氨酸结构域的¹H、¹⁵N和¹³C化学位移归属
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.
作者信息
Smal Clara, Zanzoni Serena, D'Onofrio Mariapina, Molinari Henriette, Cicero Daniel O, Assfalg Michael
机构信息
Fundación Instituto Leloir, Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina.
出版信息
Biomol NMR Assign. 2014 Oct;8(2):415-8. doi: 10.1007/s12104-013-9529-8. Epub 2013 Nov 21.
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.
在嗜冷细菌阿根廷比齐奥尼亚菌（Bizionia argentinensis）的基因组中发现了一个编码被归类为丙氨酰 - tRNA合成酶（AlaRS）的蛋白质的基因。该酶由三个具有进化保守模块化排列的结构域组成：N端氨基酰化结构域、编辑结构域和C端结构域（C - Ala）。在此，我们报告了来自阿根廷比齐奥尼亚菌的122个氨基酸的C - Ala结构域的近乎完整的核磁共振共振归属。首次报道的C - Ala结构域的化学位移数据构成了旨在阐明AlaRS冷适应机制的核磁共振结构研究的基础。
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