首页> 外文期刊>Acta crystallographica.Section D Biological crystallography. >Crystal structure and CRISPR RNA-binding site of the Cmr1 subunit of the Cmr interference complex
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Crystal structure and CRISPR RNA-binding site of the Cmr1 subunit of the Cmr interference complex

机译:晶体结构和CRISPR rna结合的地方Cmr的Cmr1单元复杂的干扰

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A multi-subunit ribonucleoprotein complex termed the Cmr RNA-silencing complex recognizes and destroys viral RNA in the CRISPR-mediated immune defence mechanism in many prokaryotes using an as yet unclear mechanism. In Archaeo-globus fulgidus, this complex consists of six subunits, Cmr1-Cmr6. Here, the crystal structure of Cmr1 from A. fulgidus is reported, revealing that the protein is composed of two tightly associated ferredoxin-like domains. The domain located at the N-terminus is structurally most similar to the N-terminal ferredoxin-like domain of the CRISPR RNA-processing enzyme Cas6 from Pyrococcus furiosus. An ensuing mutational analysis identified a highly conserved basic surface patch that binds single-stranded nucleic acids specifically, including the mature CRISPR RNA, but in a sequence-independent manner. In addition, this subunit was found to cleave single-stranded RNA. Together, these studies elucidate the structure and the catalytic activity of the Cmr1 subunit.
机译:一个multi-subunit核糖核蛋白复杂的术语Cmr RNA-silencing复杂的识别和破坏CRISPR-mediated免疫病毒RNA在许多原核生物使用的防御机制然而不清楚机制。fulgidus,这个复杂的包括六个单元,Cmr1-Cmr6。从a . fulgidus报道透露的蛋白质是由两个紧密相关的ferredoxin-like域。n端结构最相似氨基ferredoxin-like域的CRISPR rna加工酶Cas6从海床furiosus。确定一个高度保守的基本的表面补丁将单链核酸具体地说,包括成熟CRISPR RNA,但sequence-independent的方式。另外,这个亚基被发现裂开单链RNA。阐明结构和催化Cmr1单元的活动。

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