5AOX
Human Alu RNA retrotransposition complex in the ribosome-stalling conformation
Summary for 5AOX
| Entry DOI | 10.2210/pdb5aox/pdb |
| Descriptor | SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN, SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN, ALU JO CONSENSUS RNA, ... (8 entities in total) |
| Functional Keywords | translation, retrotransposition, protein targeting, rna, mobile dna, sine, line, ribonucleoprotein particle, signal recognition particle |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 6 |
| Total formula weight | 98062.62 |
| Authors | Ahl, V.,Weichenrieder, O. (deposition date: 2015-09-12, release date: 2015-11-11, Last modification date: 2024-01-10) |
| Primary citation | Ahl, V.,Keller, H.,Schmidt, S.,Weichenrieder, O. Retrotransposition and Crystal Structure of an Alu Rnp in the Ribosome-Stalling Conformation. Mol.Cell, 60:715-, 2015 Cited by PubMed Abstract: The Alu element is the most successful human genomic parasite affecting development and causing disease. It originated as a retrotransposon during early primate evolution of the gene encoding the signal recognition particle (SRP) RNA. We defined a minimal Alu RNA sufficient for effective retrotransposition and determined a high-resolution structure of its complex with the SRP9/14 proteins. The RNA adopts a compact, closed conformation that matches the envelope of the SRP Alu domain in the ribosomal translation elongation factor-binding site. Conserved structural elements in SRP RNAs support an ancient function of the closed conformation that predates SRP9/14. Structure-based mutagenesis shows that retrotransposition requires the closed conformation of the Alu ribonucleoprotein particle and is consistent with the recognition of stalled ribosomes. We propose that ribosome stalling is a common cause for the cis-preference of the mammalian L1 retrotransposon and for the efficiency of the Alu RNA in hijacking nascent L1 reverse transcriptase. PubMed: 26585389DOI: 10.1016/J.MOLCEL.2015.10.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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