3J15

Model of ribosome-bound archaeal Pelota and ABCE1

Summary for 3J15

• Entry DOI: 10.2210/pdb3j15/pdb
• Related: 3J16
• EMDB information: 2009
• Descriptor: Protein pelota, ABC transporter ATP-binding protein, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: ribosome recycling, ribosome, archaea, translation-transport protein complex, translation/transport protein
• Biological source: Thermococcus kodakarensis (Pyrococcus kodakaraensis); More
• Total number of polymer chains: 2
• Total formula weight: 109517.85

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: 2024-10-30)

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 (6.6 Å)