5LMV
Structure of bacterial 30S-IF1-IF2-IF3-mRNA-tRNA translation pre-initiation complex(state-III)
Summary for 5LMV
Entry DOI | 10.2210/pdb5lmv/pdb |
EMDB information | 4083 |
Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (29 entities in total) |
Functional Keywords | ribosome, translation, initiation factors, 30s, if1, if2, if3, trnai, pic, thermus thermophilus |
Biological source | Thermus thermophilus HB8 More |
Total number of polymer chains | 26 |
Total formula weight | 913496.63 |
Authors | Hussain, T.,Llacer, J.L.,Wimberly, B.T.,Ramakrishnan, V. (deposition date: 2016-08-01, release date: 2016-10-05, Last modification date: 2024-10-16) |
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 (4.9 Å) |
Structure validation
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