1ry1
From Proteopedia
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Structure of the signal recognition particle interacting with the elongation-arrested ribosome
Overview
Cotranslational translocation of proteins across or into membranes is a, vital process in all kingdoms of life. It requires that the translating, ribosome be targeted to the membrane by the signal recognition particle, (SRP), an evolutionarily conserved ribonucleoprotein particle. SRP, recognizes signal sequences of nascent protein chains emerging from the, ribosome. Subsequent binding of SRP leads to a pause in peptide elongation, and to the ribosome docking to the membrane-bound SRP receptor. Here we, present the structure of a targeting complex consisting of mammalian SRP, bound to an active 80S ribosome carrying a signal sequence. This, structure, solved to 12 A by cryo-electron microscopy, enables us to, generate a molecular model of SRP in its functional conformation. The, model shows how the S domain of SRP contacts the large ribosomal subunit, at the nascent chain exit site to bind the signal sequence, and that the, Alu domain reaches into the elongation-factor-binding site of the, ribosome, explaining its elongation arrest activity.
About this Structure
1RY1 is a Protein complex structure of sequences from Homo sapiens, Mus musculus, Thermus aquaticus and Tursiops truncatus. Full crystallographic information is available from OCA.
Reference
Structure of the signal recognition particle interacting with the elongation-arrested ribosome., Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R, Nature. 2004 Feb 26;427(6977):808-14. PMID:14985753
Page seeded by OCA on Mon Nov 12 19:08:15 2007
