[English] 日本語
![](img/lk-miru.gif)
- EMDB-8149: Cryo-EM structure of a full archaeal ribosomal translation initia... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-8149 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of a full archaeal ribosomal translation initiation complex in the P-INconformation | |||||||||
![]() | None | |||||||||
![]() |
| |||||||||
![]() | transcription | |||||||||
Function / homology | ![]() translation reinitiation / protein-synthesizing GTPase / formation of translation preinitiation complex / ribonuclease P activity / tRNA 5'-leader removal / translation elongation factor activity / translation initiation factor activity / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA ...translation reinitiation / protein-synthesizing GTPase / formation of translation preinitiation complex / ribonuclease P activity / tRNA 5'-leader removal / translation elongation factor activity / translation initiation factor activity / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / translational initiation / ribosome biogenesis / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / GTPase activity / mRNA binding / GTP binding / RNA binding / zinc ion binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 5.34 Å | |||||||||
![]() | COUREUX P-D / SCHMITT E | |||||||||
![]() | ![]() Title: Cryo-EM study of start codon selection during archaeal translation initiation. Authors: Pierre-Damien Coureux / Christine Lazennec-Schurdevin / Auriane Monestier / Eric Larquet / Lionel Cladière / Bruno P Klaholz / Emmanuelle Schmitt / Yves Mechulam / ![]() Abstract: Eukaryotic and archaeal translation initiation complexes have a common structural core comprising e/aIF1, e/aIF1A, the ternary complex (TC, e/aIF2-GTP-Met-tRNA) and mRNA bound to the small ribosomal ...Eukaryotic and archaeal translation initiation complexes have a common structural core comprising e/aIF1, e/aIF1A, the ternary complex (TC, e/aIF2-GTP-Met-tRNA) and mRNA bound to the small ribosomal subunit. e/aIF2 plays a crucial role in this process but how this factor controls start codon selection remains unclear. Here, we present cryo-EM structures of the full archaeal 30S initiation complex showing two conformational states of the TC. In the first state, the TC is bound to the ribosome in a relaxed conformation with the tRNA oriented out of the P site. In the second state, the tRNA is accommodated within the peptidyl (P) site and the TC becomes constrained. This constraint is compensated by codon/anticodon base pairing, whereas in the absence of a start codon, aIF2 contributes to swing out the tRNA. This spring force concept highlights a mechanism of codon/anticodon probing by the initiator tRNA directly assisted by aIF2. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 153.1 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 53.8 KB 53.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.9 KB | Display | ![]() |
Images | ![]() | 124.6 KB | ||
Filedesc metadata | ![]() | 11.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5jbhMC ![]() 8148C ![]() 5jb3C M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | None | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.12 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
+Entire : 30S archaeal translation initiation complex
+Supramolecule #1: 30S archaeal translation initiation complex
+Supramolecule #2: 30S archaeal translation initiation complex
+Supramolecule #3: 30S archaeal translation initiation complex
+Supramolecule #4: 30S archaeal translation initiation complex
+Supramolecule #5: 30S archaeal translation initiation complex
+Macromolecule #1: 16S ribosomal RNA
+Macromolecule #30: mRNA
+Macromolecule #32: initiator Met-tRNA fMet from E. coli (A1U72 variant)
+Macromolecule #2: 30S ribosomal protein uS3
+Macromolecule #3: 50S ribosomal protein uL30
+Macromolecule #4: 30S ribosomal protein uS10
+Macromolecule #5: 30S ribosomal protein uS13
+Macromolecule #6: 30S ribosomal protein uS14
+Macromolecule #7: 30S ribosomal protein eS17
+Macromolecule #8: 30S ribosomal protein uS19
+Macromolecule #9: 30S ribosomal protein eS19
+Macromolecule #10: 30S ribosomal protein eS28
+Macromolecule #11: 30S ribosomal protein eS27
+Macromolecule #12: 30S ribosomal protein uS7
+Macromolecule #13: 30S ribosomal protein uS9
+Macromolecule #14: 30S ribosomal protein uS11
+Macromolecule #15: 30S ribosomal protein uS12
+Macromolecule #16: 30S ribosomal protein uS15
+Macromolecule #17: 30S ribosomal protein uS17
+Macromolecule #18: 30S ribosomal protein uS3
+Macromolecule #19: 30S ribosomal protein uS2
+Macromolecule #20: 30S ribosomal protein eS24
+Macromolecule #21: 30S ribosomal protein eS27
+Macromolecule #22: 30S ribosomal protein uS4
+Macromolecule #23: 30S ribosomal protein eS4
+Macromolecule #24: 30S ribosomal protein uS5
+Macromolecule #25: 30S ribosomal protein eS6
+Macromolecule #26: 30S ribosomal protein uS8
+Macromolecule #27: 30S ribosomal protein eS8
+Macromolecule #28: 30S ribosomal protein SX
+Macromolecule #29: 30S ribosomal protein eL41
+Macromolecule #31: aIF1
+Macromolecule #33: aIF1A
+Macromolecule #34: aIF2-gamma
+Macromolecule #35: aIF2-beta
+Macromolecule #36: aIF2-alpha
+Macromolecule #37: METHIONINE
+Macromolecule #38: MAGNESIUM ION
+Macromolecule #39: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
+Macromolecule #40: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 44.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |