6ahu
From Proteopedia
Cryo-EM structure of human Ribonuclease P with mature tRNA
Structural highlights
Disease[POP1_HUMAN] Anauxetic dysplasia. The disease is caused by mutations affecting the gene represented in this entry. Function[RPP25_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA. [RPP40_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [RPP38_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus. [POP7_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences. [RPP30_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [POP1_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. [RPP14_HUMAN] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [RPP29_HUMAN] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P. [RPP21_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. [POP5_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP.[1] Publication Abstract from PubMedRibonuclease (RNase) P is a ubiquitous ribozyme that cleaves the 5' leader from precursor tRNAs. Here, we report cryo-electron microscopy structures of the human nuclear RNase P alone and in complex with tRNA(Val). Human RNase P is a large ribonucleoprotein complex that contains 10 protein components and one catalytic RNA. The protein components form an interlocked clamp that stabilizes the RNA in a conformation optimal for substrate binding. Human RNase P recognizes the tRNA using a double-anchor mechanism through both protein-RNA and RNA-RNA interactions. Structural comparison of the apo and tRNA-bound human RNase P reveals that binding of tRNA induces a local conformational change in the catalytic center, transforming the ribozyme into an active state. Our results also provide an evolutionary model depicting how auxiliary RNA elements in bacterial RNase P, essential for substrate binding, and catalysis, were replaced by the much more complex and multifunctional protein components in higher organisms. Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.,Wu J, Niu S, Tan M, Huang C, Li M, Song Y, Wang Q, Chen J, Shi S, Lan P, Lei M Cell. 2018 Nov 15;175(5):1393-1404.e11. doi: 10.1016/j.cell.2018.10.003. Epub, 2018 Oct 25. PMID:30454648[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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