2GO5

Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex

Summary for 2GO5

• Entry DOI: 10.2210/pdb2go5/pdb
• EMDB information: 1217
• Descriptor: SRP RNA, ribosomal RNA, Signal recognition particle 19 kDa protein (SRP19), ... (9 entities in total)
• Functional Keywords: sr, srp, ribosome, translation-rna complex, translation/rna
• Biological source: Canis sp.; More
• Cellular location: Cytoplasm: P61010; Endoplasmic reticulum membrane; Peripheral membrane protein: P08240; Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity): P47758
• Total number of polymer chains: 9
• Total formula weight: 185745.28

Authors

Halic, M.,Gartmann, M.,Schlenker, O.,Mielke, T.,Pool, M.R.,Sinning, I.,Beckmann, R. (deposition date: 2006-04-12, release date: 2006-06-13, Last modification date: 2024-10-09)

Primary citation

Halic, M.,Gartmann, M.,Schlenker, O.,Mielke, T.,Pool, M.R.,Sinning, I.,Beckmann, R.
Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site
Science, 312:745-747, 2006

PubMed Abstract: Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted.

PubMed: 16675701
DOI: 10.1126/science.1124864

Experimental method

ELECTRON MICROSCOPY (7.4 Å)