A D-amino acid editing module coupled to the translational apparatus in archaea
A D-amino acid editing module coupled to the translational apparatus in archaea
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DOI：
10.1038/nsmb943
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发表时间：
2005-06-01
影响因子：
16.8
通讯作者：
Sankaranarayanan, R
中科院分区：
文献类型：
--
作者：
Dwivedi, S;Kruparani, SP;Sankaranarayanan, R
我们报道了古细菌特定的苏酰trna合成酶编辑结构域的晶体结构，揭示了与真细菌和真核生物中发现的d -氨基酸去乙酰化酶的显著结构相似性。该结构域可以结合d -氨基酸，尽管与其他d -氨基酸脱羧酶的序列一致性较低。这些结果共同表明这些去乙酰化酶存在于所有三种生命体中。这强调了它们在翻译过程中加强同手性方面可能发挥的重要作用。
We report the crystal structure of an archaea-specific editing domain of threonyl-tRNA synthetase that reveals a marked structural similarity to D-amino acid deacylases found in eubacteria and eukaryotes. The domain can bind D-amino acids despite a low sequence identity to other D-amino acid deacylases. These results together indicate the presence of these deacylases in all three kingdoms of life. This underlines an important role they may have played in enforcing homochirality during translation.