[English] 日本語
![](img/lk-miru.gif)
- EMDB-26970: Human mitochondrial small subunit assembly intermediate (State E) -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Human mitochondrial small subunit assembly intermediate (State E) | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
Function / homology | ![]() mitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / positive regulation of mitochondrial translation / Mitochondrial translation initiation / S-adenosyl-L-methionine binding / negative regulation of mitotic nuclear division / mitochondrial small ribosomal subunit ...mitochondrial small ribosomal subunit assembly / mitochondrial ribosome binding / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation termination / positive regulation of mitochondrial translation / Mitochondrial translation initiation / S-adenosyl-L-methionine binding / negative regulation of mitotic nuclear division / mitochondrial small ribosomal subunit / mitochondrial ribosome / mitochondrial translation / positive regulation of proteolysis / ribosomal small subunit binding / Mitochondrial protein degradation / apoptotic signaling pathway / rRNA processing / cell junction / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 4 iron, 4 sulfur cluster binding / small ribosomal subunit rRNA binding / nuclear membrane / cell population proliferation / tRNA binding / rRNA binding / mitochondrial inner membrane / ribosome / structural constituent of ribosome / mitochondrial matrix / translation / protein domain specific binding / intracellular membrane-bounded organelle / mRNA binding / nucleolus / GTP binding / mitochondrion / RNA binding / nucleoplasm / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.85 Å | |||||||||
![]() | Harper NJ / Burnside C / Klinge S | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Principles of mitoribosomal small subunit assembly in eukaryotes. Authors: Nathan J Harper / Chloe Burnside / Sebastian Klinge / ![]() Abstract: Mitochondrial ribosomes (mitoribosomes) synthesize proteins encoded within the mitochondrial genome that are assembled into oxidative phosphorylation complexes. Thus, mitoribosome biogenesis is ...Mitochondrial ribosomes (mitoribosomes) synthesize proteins encoded within the mitochondrial genome that are assembled into oxidative phosphorylation complexes. Thus, mitoribosome biogenesis is essential for ATP production and cellular metabolism. Here we used cryo-electron microscopy to determine nine structures of native yeast and human mitoribosomal small subunit assembly intermediates, illuminating the mechanistic basis for how GTPases are used to control early steps of decoding centre formation, how initial rRNA folding and processing events are mediated, and how mitoribosomal proteins have active roles during assembly. Furthermore, this series of intermediates from two species with divergent mitoribosomal architecture uncovers both conserved principles and species-specific adaptations that govern the maturation of mitoribosomal small subunits in eukaryotes. By revealing the dynamic interplay between assembly factors, mitoribosomal proteins and rRNA that are required to generate functional subunits, our structural analysis provides a vignette for how molecular complexity and diversity can evolve in large ribonucleoprotein assemblies. | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 228.5 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 50.8 KB 50.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 14.1 KB | Display | ![]() |
Images | ![]() | 69.3 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Others | ![]() ![]() | 190.8 MB 191.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 928.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 928.4 KB | Display | |
Data in XML | ![]() | 21.9 KB | Display | |
Data in CIF | ![]() | 28.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8cstMC ![]() 8cspC ![]() 8csqC ![]() 8csrC ![]() 8cssC ![]() 8csuC ![]() 8d8jC ![]() 8d8kC ![]() 8d8lC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.062 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_26970_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_26970_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
+Entire : Human mitochondrial small subunit assembly intermediate, State E
+Supramolecule #1: Human mitochondrial small subunit assembly intermediate, State E
+Macromolecule #1: 28S ribosomal protein S34, mitochondrial
+Macromolecule #2: 28S ribosomal protein S35, mitochondrial
+Macromolecule #3: Aurora kinase A-interacting protein
+Macromolecule #4: Pentatricopeptide repeat domain-containing protein 3, mitochondrial
+Macromolecule #5: Putative ribosome-binding factor A, mitochondrial
+Macromolecule #6: Methyltransferase-like protein 17, mitochondrial
+Macromolecule #8: 28S ribosomal protein S2, mitochondrial
+Macromolecule #9: 28S ribosomal protein S24, mitochondrial
+Macromolecule #10: 28S ribosomal protein S5, mitochondrial
+Macromolecule #11: 28S ribosomal protein S6, mitochondrial
+Macromolecule #12: 28S ribosomal protein S7, mitochondrial
+Macromolecule #13: 28S ribosomal protein S9, mitochondrial
+Macromolecule #14: 28S ribosomal protein S10, mitochondrial
+Macromolecule #15: 28S ribosomal protein S11, mitochondrial
+Macromolecule #16: 28S ribosomal protein S12, mitochondrial
+Macromolecule #17: 28S ribosomal protein S14, mitochondrial
+Macromolecule #18: 28S ribosomal protein S15, mitochondrial
+Macromolecule #19: 28S ribosomal protein S16, mitochondrial
+Macromolecule #20: 28S ribosomal protein S17, mitochondrial
+Macromolecule #21: 28S ribosomal protein S18b, mitochondrial
+Macromolecule #22: 28S ribosomal protein S18c, mitochondrial
+Macromolecule #23: 28S ribosomal protein S21, mitochondrial
+Macromolecule #24: 28S ribosomal protein S22, mitochondrial
+Macromolecule #25: 28S ribosomal protein S23, mitochondrial
+Macromolecule #26: 28S ribosomal protein S25, mitochondrial
+Macromolecule #27: 28S ribosomal protein S26, mitochondrial
+Macromolecule #28: 28S ribosomal protein S27, mitochondrial
+Macromolecule #29: 28S ribosomal protein S28, mitochondrial
+Macromolecule #30: 28S ribosomal protein S29, mitochondrial
+Macromolecule #31: 28S ribosomal protein S31, mitochondrial
+Macromolecule #32: 28S ribosomal protein S33, mitochondrial
+Macromolecule #7: 12S mitochondrial rRNA
+Macromolecule #33: IRON/SULFUR CLUSTER
+Macromolecule #34: S-ADENOSYLMETHIONINE
+Macromolecule #35: POTASSIUM ION
+Macromolecule #36: MAGNESIUM ION
+Macromolecule #37: NICOTINAMIDE-ADENINE-DINUCLEOTIDE
+Macromolecule #38: ZINC ION
+Macromolecule #39: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #40: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #41: GUANOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 47037 / Average electron dose: 51.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.7000000000000001 µm / Nominal magnification: 64000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |