4P3G
Structure of the SRP68-RBD from Chaetomium thermophilum
Summary for 4P3G
| Entry DOI | 10.2210/pdb4p3g/pdb |
| Related | 4P3E 4P3F |
| Descriptor | Signal recognition particle subunit SRP68, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | srp, srp68, rna-binding domain (rbd), chaetomium thermophilum, tetratricopeptide repeat (tpr), rna binding protein |
| Biological source | Chaetomium thermophilum |
| Total number of polymer chains | 4 |
| Total formula weight | 100863.46 |
| Authors | Grotwinkel, J.T.,Wild, K.,Sinning, I. (deposition date: 2014-03-07, release date: 2014-04-16, Last modification date: 2024-11-13) |
| Primary citation | Grotwinkel, J.T.,Wild, K.,Segnitz, B.,Sinning, I. SRP RNA remodeling by SRP68 explains its role in protein translocation. Science, 344:101-104, 2014 Cited by PubMed Abstract: The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19. SRP68-RBD is a tetratricopeptide-like module that binds to a RNA three-way junction, bends the RNA, and inserts an α-helical arginine-rich motif (ARM) into the major groove. The ARM opens the conserved 5f RNA loop, which in ribosome-bound SRP establishes a contact to ribosomal RNA. Our data provide the structural basis for eukaryote-specific, SRP68-driven RNA remodeling required for protein translocation. PubMed: 24700861DOI: 10.1126/science.1249094 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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