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Yorodumi- EMDB-9358: Structure of human mitochondrial translation initiation factor 3 ... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-9358 | |||||||||
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Title | Structure of human mitochondrial translation initiation factor 3 bound to the small ribosomal subunit-Class-II | |||||||||
Map data | Structure of human mitochondrial translation initiation factor 3 bound to the smallribosomal subunit | |||||||||
Sample |
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Function / homology | Function and homology information Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial translational initiation / peptide biosynthetic process / mitochondrial ribosome binding / translation factor activity, RNA binding / mitochondrial ribosome assembly / ribosome disassembly / positive regulation of mitochondrial translation / Mitochondrial translation initiation ...Mitochondrial translation elongation / Mitochondrial translation termination / mitochondrial translational initiation / peptide biosynthetic process / mitochondrial ribosome binding / translation factor activity, RNA binding / mitochondrial ribosome assembly / ribosome disassembly / positive regulation of mitochondrial translation / Mitochondrial translation initiation / mitochondrial ribosome / mitochondrial small ribosomal subunit / mitochondrial translation / Mitochondrial protein degradation / ribosomal small subunit binding / translation initiation factor activity / small ribosomal subunit rRNA binding / ribosome binding / kinase activity / regulation of translation / ribosomal small subunit assembly / cell population proliferation / tRNA binding / mitochondrial inner membrane / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / apoptotic process / mitochondrion / RNA binding / nucleoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / Bovine (cattle) / Bos taurus (cattle) / Human (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.32 Å | |||||||||
Authors | Sharma M / Koripella R / Agrawal R | |||||||||
Funding support | United States, 2 items
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Citation | Journal: iScience / Year: 2019 Title: Structure of Human Mitochondrial Translation Initiation Factor 3 Bound to the Small Ribosomal Subunit. Authors: Ravi K Koripella / Manjuli R Sharma / Md Emdadul Haque / Paul Risteff / Linda L Spremulli / Rajendra K Agrawal / Abstract: The human mitochondrial translational initiation factor 3 (IF3) carries mitochondrial-specific amino acid extensions at both its N and C termini (N- and C-terminal extensions [NTE and CTE, ...The human mitochondrial translational initiation factor 3 (IF3) carries mitochondrial-specific amino acid extensions at both its N and C termini (N- and C-terminal extensions [NTE and CTE, respectively]), when compared with its eubacterial counterpart. Here we present 3.3- to 3.5-Å-resolution cryoelectron microscopic structures of the mammalian 28S mitoribosomal subunit in complex with human IF3. Unique contacts observed between the 28S subunit and N-terminal domain of IF3 explain its unusually high affinity for the 28S subunit, whereas the position of the mito-specific NTE suggests NTE's role in binding of initiator tRNA to the 28S subunit. The location of the C-terminal domain (CTD) clarifies its anti-association activity, whereas the orientation of the mito-specific CTE provides a mechanistic explanation for its role in destabilizing initiator tRNA in the absence of mRNA. Furthermore, our structure hints at a possible role of the CTD in recruiting leaderless mRNAs for translation initiation. Our findings highlight unique features of IF3 in mitochondrial translation initiation. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_9358.map.gz | 228.5 MB | EMDB map data format | |
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Header (meta data) | emd-9358-v30.xml emd-9358.xml | 42.6 KB 42.6 KB | Display Display | EMDB header |
Images | emd_9358.png | 127.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-9358 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-9358 | HTTPS FTP |
-Validation report
Summary document | emd_9358_validation.pdf.gz | 475.3 KB | Display | EMDB validaton report |
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Full document | emd_9358_full_validation.pdf.gz | 474.8 KB | Display | |
Data in XML | emd_9358_validation.xml.gz | 7.4 KB | Display | |
Data in CIF | emd_9358_validation.cif.gz | 8.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-9358 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-9358 | HTTPS FTP |
-Related structure data
Related structure data | 6neqMC 9362C 6nf8C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_9358.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Structure of human mitochondrial translation initiation factor 3 bound to the smallribosomal subunit | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07325 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : Structure of human mitochondrial translation initiation factor 3 ...
+Supramolecule #1: Structure of human mitochondrial translation initiation factor 3 ...
+Macromolecule #1: 28S ribosomal RNA, mitochondrial
+Macromolecule #2: 28S ribosomal protein S24, mitochondrial
+Macromolecule #3: 28S ribosomal protein S5, mitochondrial
+Macromolecule #4: 28S ribosomal protein S12, mitochondrial
+Macromolecule #5: 28S ribosomal protein S16, mitochondrial
+Macromolecule #6: 28S ribosomal protein S17, mitochondrial
+Macromolecule #7: 28S ribosomal protein S22, mitochondrial
+Macromolecule #8: 28S ribosomal protein S25, mitochondrial
+Macromolecule #9: 28S ribosomal protein S26, mitochondrial
+Macromolecule #10: 28S ribosomal protein S27, mitochondrial
+Macromolecule #11: 28S ribosomal protein S34, mitochondrial
+Macromolecule #12: 28S ribosomal protein S18b, mitochondrial
+Macromolecule #13: 28S ribosomal protein S7, mitochondrial
+Macromolecule #14: 28S ribosomal protein S9, mitochondrial
+Macromolecule #15: 28S ribosomal protein S10, mitochondrial
+Macromolecule #16: 28S ribosomal protein S14, mitochondrial
+Macromolecule #17: DAP3 protein
+Macromolecule #18: 28S ribosomal protein S31, mitochondrial
+Macromolecule #19: 28S ribosomal protein S33, mitochondrial
+Macromolecule #20: 28S ribosomal protein S35, mitochondrial
+Macromolecule #21: Coiled-coil-helix-coiled-coil-helix domain containing 1
+Macromolecule #22: Pentatricopeptide repeat domain-containing protein 3, mitochondrial
+Macromolecule #23: 28S ribosomal protein S2, mitochondrial
+Macromolecule #24: 28S ribosomal protein S6, mitochondrial
+Macromolecule #25: 28S ribosomal protein S11, mitochondrial
+Macromolecule #26: 28S ribosomal protein S15, mitochondrial
+Macromolecule #27: 28S ribosomal protein S18c, mitochondrial
+Macromolecule #28: 28S ribosomal protein S21, mitochondrial
+Macromolecule #29: 28S ribosomal protein S23, mitochondrial
+Macromolecule #30: 28S ribosomal protein S28, mitochondrial
+Macromolecule #31: Aurora kinase A interacting protein 1
+Macromolecule #32: Translation initiation factor IF-3, mitochondrial
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 70.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: OTHER |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.32 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 198355 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |