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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability
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Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability

机译：Aeropyrum pernix L7Ae多功能蛋白的结构及其极高的热稳定性的见解

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摘要

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 angstrom. 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.
机译：古细菌核糖体蛋白L7Ae是一种多功能RNA结合蛋白，可指导古细菌RNA的转录后修饰。发现来自Cernarchaea的Aeropyrum pernix的L7Ae蛋白（Ap L7Ae）具有极高的解链温度（> 383 K）。 Ap L7Ae的晶体结构已确定为分辨率为1.56埃。将Ap L7Ae的结构与两个同源物的结构进行了比较：嗜温性詹氏甲烷球菌L7Ae和相应的嗜温性哺乳动物15.5 kD蛋白。 Ap L7Ae蛋白的主要稳定功能似乎是大量的离子对和连接二级结构元件的广泛的离子对网络。据我们所知，Ap L7Ae是目前观察到的最热稳定的单结构域单体蛋白之一。

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