Science. 2006 May 5;312(5774):745-7.

Signal recognition particle receptor exposes the ribosomal translocon binding site.

Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R.

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Institute of Biochemistry, Charité, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany.

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.

PMID:: 16675701; [PubMed - indexed for MEDLINE]

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Structure of the signal recognition particle interacting with the elongation-arrested ribosome. [Nature. 2004]
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Cited by 23 PubMed Central articles

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Braig D, Mircheva M, Sachelaru I, van der Sluis EO, Sturm L, Beckmann R, Koch HG. Mol Biol Cell. 2011 Jul 1; 22(13):2309-23. Epub 2011 May 5.
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Structures reported by this article

Structure Of Signal Recognition Particle Receptor (Sr) In Complex With Signal Recognition Particle (Srp) And Ribosome Nascent Chain Complex

PDB: 2GO5

Source: Canis sp., Homo sapiens, Mus musculus, Triticum sp.

Method: Cryo-Electron Microscopy

Resolution: 7.4 Å

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