EMD-4075

Single-particle
5.35 Å
EMD-4075 Deposition: 01/08/2016
Map released: 05/10/2016
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-4075

Structure of bacterial 30S-IF1-IF3-mRNA translation pre-initiation complex (state-1C)

EMD-4075

Single-particle
5.35 Å
EMD-4075 Deposition: 01/08/2016
Map released: 05/10/2016
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Thermus thermophilus
Sample: 30S-IF1-IF3-mRNA pre-initiation complex (state-1C)
Fitted models: 5lmp (Avg. Q-score: 0.213)

Deposition Authors: Hussain T , Llacer JL
Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation.
Hussain T , Llacer JL , Wimberly BT, Kieft JS, Ramakrishnan V
(2016) Cell , 167 , 133 - 144.e13
PUBMED: 27662086
DOI: doi:10.1016/j.cell.2016.08.074
ISSN: 1097-4172
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.