5LW7
S. solfataricus ABCE1 post-splitting state
Summary for 5LW7
| Entry DOI | 10.2210/pdb5lw7/pdb |
| Related | 4V6U |
| EMDB information | 4113 |
| Descriptor | ABC transporter ATP-binding protein, IRON/SULFUR CLUSTER (2 entities in total) |
| Functional Keywords | abce1, recycling, 30s, ribosome |
| Biological source | Pyrococcus abyssi (strain GE5 / Orsay) |
| Total number of polymer chains | 1 |
| Total formula weight | 67989.55 |
| Authors | Heuer, A.,Gerovac, M.,Beckmann, R.,Tampe, R. (deposition date: 2016-09-15, release date: 2016-11-16, Last modification date: 2024-11-13) |
| Primary citation | Kiosze-Becker, K.,Ori, A.,Gerovac, M.,Heuer, A.,Nurenberg-Goloub, E.,Rashid, U.J.,Becker, T.,Beckmann, R.,Beck, M.,Tampe, R. Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry. Nat Commun, 7:13248-13248, 2016 Cited by PubMed Abstract: Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final-or the first-step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S·ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix-loop-helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling. PubMed: 27824037DOI: 10.1038/ncomms13248 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (17 Å) |
Structure validation
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