3j15

Model of ribosome-bound archaeal Pelota and ABCE1

Loading... Status: waiting for Mol* initialization Structural highlights 3j15 is a 2 chain structure with sequence from Pyrococcus furiosus and Thermococcus kodakarensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 6.6Å Ligands: ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PELO_THEKO May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity (By similarity). Publication Abstract from PubMed Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryo-electron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.,Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache JP, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, Karcher A, Thomm M, Hopfner KP, Green R, Beckmann R Nature. 2012 Feb 22;482(7386):501-6. doi: 10.1038/nature10829. PMID:22358840 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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