title: Signal recognition particle receptor exposes the ribosomal translocon binding site.
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.
authors: Institute of Biochemistry, Charité, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany.
authors: Mario
authors: M
authors: Halic
authors: Marco
authors: M
authors: Gartmann
authors: Oliver
authors: O
authors: Schlenker
authors: Thorsten
authors: T
authors: Mielke
authors: Martin R
authors: MR
authors: Pool
authors: Irmgard
authors: I
authors: Sinning
authors: Roland
authors: R
authors: Beckmann