2OB7
Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM
Summary for 2OB7
| Entry DOI | 10.2210/pdb2ob7/pdb |
| Related | 1N34 1PV6 1Q2B |
| EMDB information | 1310 1311 1312 |
| Descriptor | transfer-messenger RNA, 16S ribosomal RNA, SsrA-binding protein (3 entities in total) |
| Functional Keywords | tmrna, smpb, rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 4 |
| Total formula weight | 170597.87 |
| Authors | Frank, J.,Felden, B.,Gillet, R.,Li, W. (deposition date: 2006-12-18, release date: 2007-01-23, Last modification date: 2023-12-27) |
| Primary citation | Gillet, R.,Kaur, S.,Li, W.,Hallier, M.,Felden, B.,Frank, J. Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1. J.Biol.Chem., 282:6356-6363, 2007 Cited by PubMed Abstract: A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation. PubMed: 17179154DOI: 10.1074/jbc.M609658200 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13.6 Å) |
Structure validation
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