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Yorodumi- EMDB-17699: Structure of human 48S translation initiation complex after eIF5 ... -
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Open data
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Basic information
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| Title | Structure of human 48S translation initiation complex after eIF5 release (48S-4) | |||||||||
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Keywords | RIBOSOME / TRANSLATION / initiation / 48S / eIF / human / eukaryotic / factor / codon / scanning / closed | |||||||||
| Function / homology | Function and homology informationpositive regulation of mRNA binding / translation initiation ternary complex / regulation of translation in response to endoplasmic reticulum stress / glial limiting end-foot / HRI-mediated signaling / viral translational termination-reinitiation / response to manganese-induced endoplasmic reticulum stress / Cellular response to mitochondrial stress / positive regulation of type B pancreatic cell apoptotic process / eukaryotic translation initiation factor 3 complex, eIF3e ...positive regulation of mRNA binding / translation initiation ternary complex / regulation of translation in response to endoplasmic reticulum stress / glial limiting end-foot / HRI-mediated signaling / viral translational termination-reinitiation / response to manganese-induced endoplasmic reticulum stress / Cellular response to mitochondrial stress / positive regulation of type B pancreatic cell apoptotic process / eukaryotic translation initiation factor 3 complex, eIF3e / Response of EIF2AK1 (HRI) to heme deficiency / Recycling of eIF2:GDP / negative regulation of translational initiation in response to stress / cap-dependent translational initiation / methionyl-initiator methionine tRNA binding / eukaryotic translation initiation factor 3 complex, eIF3m / PERK-mediated unfolded protein response / PERK regulates gene expression / IRES-dependent viral translational initiation / response to kainic acid / translation reinitiation / eukaryotic translation initiation factor 2 complex / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / cytoplasmic translational initiation / multi-eIF complex / regulation of translational initiation in response to stress / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / mRNA cap binding / formation of translation preinitiation complex / eukaryotic 48S preinitiation complex / oxidized pyrimidine DNA binding / response to TNF agonist / negative regulation of endoplasmic reticulum unfolded protein response / positive regulation of base-excision repair / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of DNA repair / negative regulation of RNA splicing / metal-dependent deubiquitinase activity / supercoiled DNA binding / neural crest cell differentiation / protein-synthesizing GTPase / NF-kappaB complex / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / cysteine-type endopeptidase activator activity involved in apoptotic process / regulation of translational initiation / oxidized purine DNA binding / positive regulation of ubiquitin-protein transferase activity / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / regulation of establishment of cell polarity / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / negative regulation of phagocytosis / rRNA modification in the nucleus and cytosol / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / negative regulation of ubiquitin protein ligase activity / protein kinase A binding / ion channel inhibitor activity / Ribosomal scanning and start codon recognition / pigmentation / Translation initiation complex formation / positive regulation of mitochondrial depolarization / positive regulation of T cell receptor signaling pathway / negative regulation of Wnt signaling pathway / fibroblast growth factor binding / monocyte chemotaxis / positive regulation of activated T cell proliferation / negative regulation of translational frameshifting / TOR signaling / Protein hydroxylation / BH3 domain binding / SARS-CoV-1 modulates host translation machinery / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / cellular response to ethanol / regulation of cell division / iron-sulfur cluster binding / mTORC1-mediated signalling / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / positive regulation of GTPase activity / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / negative regulation of ubiquitin-dependent protein catabolic process Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Petrychenko V / Yi S-H / Liedtke D / Peng BZ / Rodnina MV / Fischer N | |||||||||
| Funding support | Germany, 2 items
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Citation | Journal: Protein Sci / Year: 2018 Title: UCSF ChimeraX: Meeting modern challenges in visualization and analysis. Authors: Thomas D Goddard / Conrad C Huang / Elaine C Meng / Eric F Pettersen / Gregory S Couch / John H Morris / Thomas E Ferrin / ![]() Abstract: UCSF ChimeraX is next-generation software for the visualization and analysis of molecular structures, density maps, 3D microscopy, and associated data. It addresses challenges in the size, scope, and ...UCSF ChimeraX is next-generation software for the visualization and analysis of molecular structures, density maps, 3D microscopy, and associated data. It addresses challenges in the size, scope, and disparate types of data attendant with cutting-edge experimental methods, while providing advanced options for high-quality rendering (interactive ambient occlusion, reliable molecular surface calculations, etc.) and professional approaches to software design and distribution. This article highlights some specific advances in the areas of visualization and usability, performance, and extensibility. ChimeraX is free for noncommercial use and is available from http://www.rbvi.ucsf.edu/chimerax/ for Windows, Mac, and Linux. | |||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_17699.map.gz | 275 MB | EMDB map data format | |
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| Header (meta data) | emd-17699-v30.xml emd-17699.xml | 86.1 KB 86.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_17699_fsc.xml | 12.7 KB | Display | FSC data file |
| Images | emd_17699.png | 187.7 KB | ||
| Masks | emd_17699_msk_1.map | 178 MB | Mask map | |
| Filedesc metadata | emd-17699.cif.gz | 20.1 KB | ||
| Others | emd_17699_additional_1.map.gz emd_17699_additional_2.map.gz emd_17699_additional_3.map.gz emd_17699_half_map_1.map.gz emd_17699_half_map_2.map.gz | 163.4 MB 162.4 MB 140.6 MB 140.7 MB 140.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17699 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17699 | HTTPS FTP |
-Validation report
| Summary document | emd_17699_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_17699_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_17699_validation.xml.gz | 21.9 KB | Display | |
| Data in CIF | emd_17699_validation.cif.gz | 27.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17699 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17699 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8pj4MC ![]() 8pj1C ![]() 8pj2C ![]() 8pj3C ![]() 8pj5C ![]() 8pj6C ![]() 8rg0C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_17699.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.967 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_17699_msk_1.map | ||||||||||||
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-Additional map: eIF2-GDP substate 1 (48S-4-1)
| File | emd_17699_additional_1.map | ||||||||||||
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| Annotation | eIF2-GDP substate 1 (48S-4-1) | ||||||||||||
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-Additional map: eIF2-GDP substate 2 (48S-4-2)
| File | emd_17699_additional_2.map | ||||||||||||
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| Annotation | eIF2-GDP substate 2 (48S-4-2) | ||||||||||||
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| Density Histograms |
-Additional map: Unsharpened main map from 3D refinement step
| File | emd_17699_additional_3.map | ||||||||||||
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| Annotation | Unsharpened main map from 3D refinement step | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_17699_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_17699_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Human 48S initiation complex 40S-eIF1A-eIF2-eIF3-eIF5B-tRNA-Met-mRNA
+Supramolecule #1: Human 48S initiation complex 40S-eIF1A-eIF2-eIF3-eIF5B-tRNA-Met-mRNA
+Macromolecule #1: Eukaryotic translation initiation factor 5B
+Macromolecule #2: Eukaryotic translation initiation factor 3 subunit B
+Macromolecule #3: Eukaryotic translation initiation factor 3 subunit I
+Macromolecule #4: Eukaryotic translation initiation factor 3 subunit K
+Macromolecule #5: Eukaryotic translation initiation factor 3 subunit F
+Macromolecule #6: Eukaryotic translation initiation factor 3 subunit L
+Macromolecule #7: Eukaryotic translation initiation factor 3 subunit M
+Macromolecule #9: Eukaryotic translation initiation factor 3 subunit H
+Macromolecule #10: 60S ribosomal protein L41
+Macromolecule #12: 40S ribosomal protein S11
+Macromolecule #13: 40S ribosomal protein S4, X isoform
+Macromolecule #14: 40S ribosomal protein S9
+Macromolecule #15: 40S ribosomal protein S23
+Macromolecule #16: Small ribosomal subunit protein eS30
+Macromolecule #17: 40S ribosomal protein S7
+Macromolecule #18: 40S ribosomal protein S27
+Macromolecule #19: 40S ribosomal protein S13
+Macromolecule #20: 40S ribosomal protein S15a
+Macromolecule #21: 40S ribosomal protein S21
+Macromolecule #22: 40S ribosomal protein S2
+Macromolecule #23: 40S ribosomal protein S17
+Macromolecule #24: 40S ribosomal protein SA
+Macromolecule #25: 40S ribosomal protein S3a
+Macromolecule #26: 40S ribosomal protein S14
+Macromolecule #27: 40S ribosomal protein S26
+Macromolecule #28: 40S ribosomal protein S8
+Macromolecule #29: 40S ribosomal protein S6
+Macromolecule #30: 40S ribosomal protein S24
+Macromolecule #31: 40S ribosomal protein S5
+Macromolecule #32: 40S ribosomal protein S16
+Macromolecule #33: 40S ribosomal protein S3
+Macromolecule #34: 40S ribosomal protein S10
+Macromolecule #35: 40S ribosomal protein S15
+Macromolecule #36: Receptor of activated protein C kinase 1
+Macromolecule #37: 40S ribosomal protein S19
+Macromolecule #38: 40S ribosomal protein S25
+Macromolecule #39: 40S ribosomal protein S18
+Macromolecule #40: 40S ribosomal protein S20
+Macromolecule #41: 40S ribosomal protein S29
+Macromolecule #42: Ubiquitin
+Macromolecule #43: 40S ribosomal protein S12
+Macromolecule #44: 40S ribosomal protein S28
+Macromolecule #45: Eukaryotic translation initiation factor 3 subunit G
+Macromolecule #46: Eukaryotic translation initiation factor 1A, X-chromosomal
+Macromolecule #47: Eukaryotic translation initiation factor 2 subunit 1
+Macromolecule #48: Eukaryotic translation initiation factor 2 subunit 3
+Macromolecule #49: Eukaryotic translation initiation factor 3 subunit A
+Macromolecule #50: Eukaryotic translation initiation factor 3 subunit E
+Macromolecule #52: Eukaryotic translation initiation factor 3 subunit D
+Macromolecule #53: Eukaryotic translation initiation factor 3 subunit C
+Macromolecule #8: mRNA
+Macromolecule #11: 18S rRNA
+Macromolecule #51: Initiator Met-tRNA-i
+Macromolecule #54: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #55: SODIUM ION
+Macromolecule #56: MAGNESIUM ION
+Macromolecule #57: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 Component:
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| Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER / Details: Manual blotting & plunge-freezing. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Spherical aberration corrector: Electron-optical aberrations were corrected using a CETCOR Cs-corrector (CEOS, Heidelberg) aligned with the CETCORPLUS 4.6.9 software package (CEOS, Heidelberg). |
| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average exposure time: 1.5 sec. / Average electron dose: 45.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.2 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 |
Movie
Controller
About Yorodumi



Keywords
Homo sapiens (human)
Authors
Germany, 2 items
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Processing
FIELD EMISSION GUN

