3J16

Models of ribosome-bound Dom34p and Rli1p and their ribosomal binding partners

Summary for 3J16

• Entry DOI: 10.2210/pdb3j16/pdb
• Related: 3J15
• EMDB information: 2008 2010
• Descriptor: Dom34p, 60S ribosomal protein L11, 40S ribosomal protein S24E, ... (16 entities in total)
• Functional Keywords: ribosome recycling, translation, eukarya, ribosome
• Biological source: Saccharomyces cerevisiae; More
• Cellular location: Cytoplasm: P33309 Q03195 P05738 P0CX33 P0CX37 P0CX53 P0CX31; Cytoplasm (By similarity): P05317 P0CX41
• Total number of polymer chains: 12
• Total formula weight: 400146.83

Authors

Becker, T.,Franckenberg, S.,Wickles, S.,Shoemaker, C.J.,Anger, A.M.,Armache, J.-P.,Sieber, H.,Ungewickell, C.,Berninghausen, O.,Daberkow, I.,Karcher, A.,Thomm, M.,Hopfner, K.-P.,Green, R.,Beckmann, R. (deposition date: 2011-12-12, release date: 2012-02-22, Last modification date: 2024-02-21)

Primary citation

Becker, T.,Franckenberg, S.,Wickles, S.,Shoemaker, C.J.,Anger, A.M.,Armache, J.-P.,Sieber, H.,Ungewickell, C.,Berninghausen, O.,Daberkow, I.,Karcher, A.,Thomm, M.,Hopfner, K.P.,Green, R.,Beckmann, R.
Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.
Nature, 482:501-506, 2012

PubMed Abstract: 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.

PubMed: 22358840
DOI: 10.1038/nature10829

Experimental method

ELECTRON MICROSCOPY (7.2 Å)