Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.
Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.
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Aeropyrum pernix L7Ae 多功能蛋白的结构及其极端热稳定性的见解。
DOI：
10.1107/s1744309113021799
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Brown2nd,BernardAndrew
中科院分区：
文献类型：
--
作者：
Bhuiya,MohammadWadud;Suryadi,Jimmy;Zhou,Zholi;Brown2nd,BernardAndrew
古细菌核糖体蛋白L7Ae是一种多功能的RNA结合蛋白，指导古细菌RNA的转录后修饰。来自泉古菌Aeropyrum pernix（Ap L7Ae）的L7Ae蛋白具有极高的解链温度（>383 K）。 测定了Ap L7Ae的晶体结构，其分辨率为1.56 μ m。 Ap L7Ae的结构与两个同源物的结构进行了比较：超嗜热的詹氏甲烷球菌L7Ae和嗜温的对应哺乳动物15.5 kD蛋白。 Ap L7Ae蛋白的主要稳定特征似乎是连接二级结构元件的大量离子对和广泛的离子对网络。据我们所知，Ap L7Ae是目前观察到的最耐热的单结构域单体蛋白之一。
Archaeal ribosomal protein L7Ae is a multifunctional RNA-binding protein that directs post-transcriptional modification of archaeal RNAs. The L7Ae protein from Aeropyrum pernix (Ap L7Ae), a member of the Crenarchaea, was found to have an extremely high melting temperature (>383 K). The crystal structure of Ap L7Ae has been determined to a resolution of 1.56 Å. The structure of Ap L7Ae was compared with the structures of two homologs: hyperthermophilic Methanocaldococcus jannaschii L7Ae and the mesophilic counterpart mammalian 15.5 kD protein. The primary stabilizing feature in the Ap L7Ae protein appears to be the large number of ion pairs and extensive ion-pair network that connects secondary-structural elements. To our knowledge, Ap L7Ae is among the most thermostable single-domain monomeric proteins presently observed.