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2go5

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2go5, resolution 7.40Å ()
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

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

Publication Abstract from PubMed

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.

Signal recognition particle receptor exposes the ribosomal translocon binding site., Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R, Science. 2006 May 5;312(5774):745-7. PMID:16675701

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2go5 is a 9 chain structure with sequence from Canis sp., Homo sapiens, Mus musculus and Triticum sp.. Full crystallographic information is available from OCA.

See Also

Reference

  • Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science. 2006 May 5;312(5774):745-7. PMID:16675701 doi:312/5774/745

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