5LMU
Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form (state-4)
Summary for 5LMU
| Entry DOI | 10.2210/pdb5lmu/pdb |
| EMDB information | 4080 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (26 entities in total) |
| Functional Keywords | ribosome, translation, initiation factors, 30s, if1, if3, trnai, pic, thermus thermophilus |
| Biological source | Thermus thermophilus HB8 More |
| Total number of polymer chains | 24 |
| Total formula weight | 843702.17 |
| Authors | Hussain, T.,Llacer, J.L.,Wimberly, B.T.,Ramakrishnan, V. (deposition date: 2016-08-01, release date: 2016-10-05, Last modification date: 2024-05-15) |
| Primary citation | Hussain, T.,Llacer, J.L.,Wimberly, B.T.,Kieft, J.S.,Ramakrishnan, V. Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation. Cell, 167:133-144.e13, 2016 Cited by PubMed Abstract: In bacterial translational initiation, three initiation factors (IFs 1-3) enable the selection of initiator tRNA and the start codon in the P site of the 30S ribosomal subunit. Here, we report 11 single-particle cryo-electron microscopy (cryoEM) reconstructions of the complex of bacterial 30S subunit with initiator tRNA, mRNA, and IFs 1-3, representing different steps along the initiation pathway. IF1 provides key anchoring points for IF2 and IF3, thereby enhancing their activities. IF2 positions a domain in an extended conformation appropriate for capturing the formylmethionyl moiety charged on tRNA. IF3 and tRNA undergo large conformational changes to facilitate the accommodation of the formylmethionyl-tRNA (fMet-tRNA(fMet)) into the P site for start codon recognition. PubMed: 27662086DOI: 10.1016/j.cell.2016.08.074 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
Download full validation report
