Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
复制标题
DOI：
10.1038/nsmb1047
复制
发表时间：
2006-02-01
影响因子：
16.8
通讯作者：
Verdine, GL
中科院分区：
文献类型：
--
作者：
Losey, HC;Ruthenburg, AJ;Verdine, GL
细菌tRNA腺苷脱氨酶（TadAs）在tRNA的摆动位置（Arg2）催化腺苷水解脱氨为肌苷，这一过程使单个tRNA能够识别mRNA中三种不同的精氨酸密码子。此外，肌苷也被引入到多个真核trna的摆动位置。编码这些脱氨酶的基因在细菌和酵母中是必不可少的，证明了它们的生物活性的重要性。本文报道了金黄色葡萄球菌TadA在2.0埃的结晶和结构测定，该TadA与tRNAArg2的反密码子茎环结合，在摆动位置含有nebularine（一种不可水解的腺苷类似物）。共晶结构揭示了TadA与RNA相互作用中序列和结构特异性的基础，并进一步揭示了促进高效水解脱氨的活性位点结构。
Bacterial tRNA adenosine deaminases (TadAs) catalyze the hydrolytic deamination of adenosine to inosine at the wobble position of tRNA(Arg2), a process that enables this single tRNA to recognize three different arginine codons in mRNA. In addition, inosine is also introduced at the wobble position of multiple eukaryotic tRNAs. The genes encoding these deaminases are essential in bacteria and yeast, demonstrating the importance of their biological activity. Here we report the crystallization and structure determination to 2.0 angstrom of Staphylococcus aureus TadA bound to the anticodon stem-loop of tRNAArg2 bearing nebularine, a non-hydrolyzable adenosine analog, at the wobble position. The cocrystal structure reveals the basis for both sequence and structure specificity in the interactions of TadA with RNA, and it additionally provides insight into the active site architecture that promotes efficient hydrolytic deamination.