4P3F

Structure of the human SRP68-RBD

Summary for 4P3F

• Entry DOI: 10.2210/pdb4p3f/pdb
• Related: 4P3E 4P3G
• Descriptor: Signal recognition particle subunit SRP68, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: srpsrp68rna-binding domain (rbd), tetratricopeptide repeat (tpr), rna binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 51775.09

Authors

Grotwinkel, J.T.,Wild, K.,Sinning, I. (deposition date: 2014-03-07, release date: 2014-04-16, Last modification date: 2023-09-27)

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

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: 24700861
DOI: 10.1126/science.1249094

Experimental method

X-RAY DIFFRACTION (1.699 Å)