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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.
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Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.

机译：Methanothermobacter结构thermautotrophicus外来体核糖核酸酶PH戒指。

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摘要

The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial polynucleotide phosphorylase (PNPase). While all six RNase PH monomers are catalytically active in the homohexameric RNase PH, only half of them are functional in the bacterial PNPase and in the archaeal exosome core and none are functional in the yeast and human exosome cores. Here, the crystal structure of the RNase PH ring from the exosome of the anaerobic methanogenic archaeon Methanothermobacter thermautotrophicus is described at 2.65 A resolution. Free phosphate anions were found for the first time in the active sites of the RNase PH subunits of an exosome structure and provide structural snapshots of a critical intermediate in the phosphorolytic degradation of RNA by the exosome. Furthermore, the present structure highlights the plasticity of the surfaces delineating the polar regions of the RNase PH ring of the exosome, a feature that can facilitate both interaction with the many cofactors involved in exosome function and the processive activity of this enzyme.
机译：多功能multisubunit外来体的核心在古菌和rna加工酶的发现真核生物,包括一个六环核糖核酸酶的PH值子单元。细菌和古细菌核糖核酸酶的小灵通和细菌多核苷酸磷酸化酶(PNPase)。催化地活跃于homohexameric核糖核酸酶PH值,其中只有一半是功能性的PNPase细菌和古细菌外来体核心并在酵母和人类没有的功能外来体核。从厌氧的外来体核糖核酸酶PH值环产甲烷archaeon Methanothermobacter在2.65 thermautotrophicus描述决议。第一次在核糖核酸酶的活性区域PH值子单元的外来体结构和提供结构快照的一个关键的中间在phosphorolytic RNA的降解外来体。突出表面的可塑性描述的极地核糖核酸酶的PH值环的外来体,一个功能,可以促进与许多交互代数余子式和参与外来体功能进行的这种酶的活性。

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