1E8S

Alu domain of the mammalian SRP (potential Alu retroposition intermediate)

Summary for 1E8S

• Entry DOI: 10.2210/pdb1e8s/pdb
• Related: 1E8O
• Descriptor: SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN, SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN, 7SL RNA, 88-MER, ... (4 entities in total)
• Functional Keywords: alu ribonucleoprotein particle, alu rnp assembly and dimerisation, translational control, alu retroposition
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: P49458 P37108
• Total number of polymer chains: 3
• Total formula weight: 50905.63

Authors

Weichenrieder, O.,Wild, K.,Strub, K.,Cusack, S. (deposition date: 2000-09-29, release date: 2000-11-08, Last modification date: 2024-05-08)

Primary citation

Weichenrieder, O.,Wild, K.,Strub, K.,Cusack, S.
Structure and Assembly of the Alu Domain of the Mammalian Signal Recognition Particle
Nature, 408:167-, 2000

PubMed Abstract: The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. It retards the ribosomal elongation of signal-peptide-containing proteins before their engagement with the translocation machinery in the endoplasmic reticulum. Here we report two crystal structures of the heterodimer SRP9/14 bound either to the 5' domain or to a construct containing both 5' and 3' domains. We present a model of the complete Alu domain that is consistent with extensive biochemical data. SRP9/14 binds strongly to the conserved core of the 5' domain, which forms a U-turn connecting two helical stacks. Reversible docking of the more weakly bound 3' domain might be functionally important in the mechanism of translational regulation. The Alu domain structure is probably conserved in other cytoplasmic ribonucleoprotein particles and retroposition intermediates containing SRP9/14-bound RNAs transcribed from Alu repeats or related elements in genomic DNA.

PubMed: 11089964
DOI: 10.1038/35041507

Experimental method

X-RAY DIFFRACTION (4 Å)