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5AOX

Human Alu RNA retrotransposition complex in the ribosome-stalling conformation

Summary for 5AOX
Entry DOI10.2210/pdb5aox/pdb
DescriptorSIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN, SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN, ALU JO CONSENSUS RNA, ... (8 entities in total)
Functional Keywordstranslation, retrotransposition, protein targeting, rna, mobile dna, sine, line, ribonucleoprotein particle, signal recognition particle
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains6
Total formula weight98062.62
Authors
Ahl, V.,Weichenrieder, O. (deposition date: 2015-09-12, release date: 2015-11-11, Last modification date: 2024-01-10)
Primary citationAhl, 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: 26585389
DOI: 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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