首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum
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Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum

机译:嗜热真核生物嗜热小球菌剪接体RNA解旋酶Prp28的结构分析

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摘要

Prp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6·U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5′-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 Å resolution and is compared with the available structures of homologues.
机译:Prp28(mRNA剪接前的ATP依赖性RNA解旋酶28)是一种剪接体DEAD-box解旋酶,它参与剪接体组装的两个步骤。以ATP非依赖性的方式形成承诺复合物2以及形成与ATP呈依赖性的催化前剪接体是必需的。在后面的步骤中,Prp28对U4 / U6·U5 tri-snRNP的整合至关重要,因为它取代了U1 snRNP,并使U6 snRNP与5'剪接位点碱基配对。在此,据报道嗜热真菌嗜热Chaetomium thermophilum的Prp28的晶体结构的分辨率为3.2Å,并与可用的同源物结构进行了比较。

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