5lmu

Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form (state-4)Structure of bacterial 30S-IF3-mRNA-tRNA translation pre-initiation complex, closed form (state-4)

5lmu, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 5lmu is a 10 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS2_THET8 Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B] Publication Abstract from PubMed 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. Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation.,Hussain T, Llacer JL, Wimberly BT, Kieft JS, Ramakrishnan V Cell. 2016 Sep 22;167(1):133-144.e13. doi: 10.1016/j.cell.2016.08.074. PMID:27662086 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein THX 3D structures