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- EMDB-4082: Structure of bacterial 30S-IF1-IF2-IF3-mRNA-tRNA translation pre-... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-4082 | |||||||||
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Title | Structure of bacterial 30S-IF1-IF2-IF3-mRNA-tRNA translation pre-initiation complex(state-II) | |||||||||
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Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.3 Å | |||||||||
![]() | Hussain T / Llacer JL / Wimberly BT / Ramakrishnan V | |||||||||
![]() | ![]() Title: Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation. Authors: Tanweer Hussain / Jose L Llácer / Brian T Wimberly / Jeffrey S Kieft / V Ramakrishnan / ![]() ![]() 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 ...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. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 62.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20 KB 20 KB | Display Display | ![]() |
Images | ![]() | 152 KB | ||
Others | ![]() ![]() | 58.5 MB 58.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 419.8 KB | Display | ![]() |
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Full document | ![]() | 419 KB | Display | |
Data in XML | ![]() | 11 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4073C ![]() 4074C ![]() 4075C ![]() 4076C ![]() 4077C ![]() 4078C ![]() 4079C ![]() 4080C ![]() 4081C ![]() 4083C ![]() 5lmnC ![]() 5lmoC ![]() 5lmpC ![]() 5lmqC ![]() 5lmrC ![]() 5lmsC ![]() 5lmtC ![]() 5lmuC ![]() 5lmvC C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: #1
File | emd_4082_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_4082_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : 30S-IF1-IF2-IF3-mRNA-tRNA pre-initiation complex (state-II)
Entire | Name: 30S-IF1-IF2-IF3-mRNA-tRNA pre-initiation complex (state-II) |
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Components |
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-Supramolecule #1: 30S-IF1-IF2-IF3-mRNA-tRNA pre-initiation complex (state-II)
Supramolecule | Name: 30S-IF1-IF2-IF3-mRNA-tRNA pre-initiation complex (state-II) type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#26 |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 912.9 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.065 mg/mL | ||||||||||||
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Buffer | pH: 6.5 Component:
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Grid | Model: Quantifoil / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK I |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Temperature | Min: 90.0 K / Max: 100.0 K |
Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Number grids imaged: 1 / Number real images: 3200 / Average exposure time: 1.5 sec. / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 104478 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: RECIPROCAL / Protocol: OTHER / Target criteria: FSC |
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