4p3e

Structure of the human SRP S domain

spinqualitylabelsall models 4p3e, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p3e is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 4p3f, 4p3g Gene: SRP19 (HUMAN), SRP68 (HUMAN) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 alpha-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. SRP RNA remodeling by SRP68 explains its role in protein translocation.,Grotwinkel JT, Wild K, Segnitz B, Sinning I Science. 2014 Apr 4;344(6179):101-4. doi: 10.1126/science.1249094. PMID:24700861 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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