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Yorodumi- EMDB-23939: Cryo-EM structure of the human SSU processome, state pre-A1 - raw maps -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-23939 | |||||||||
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Title | Cryo-EM structure of the human SSU processome, state pre-A1 - raw maps | |||||||||
Map data | Main map | |||||||||
Sample |
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Function / homology | Function and homology information mRNA N-acetyltransferase activity / negative regulation of superoxide anion generation / preribosome / oocyte growth / nucleologenesis / U4atac snRNP / rRNA acetylation involved in maturation of SSU-rRNA / rRNA cytidine N-acetyltransferase activity / snoRNA localization / leucine zipper domain binding ...mRNA N-acetyltransferase activity / negative regulation of superoxide anion generation / preribosome / oocyte growth / nucleologenesis / U4atac snRNP / rRNA acetylation involved in maturation of SSU-rRNA / rRNA cytidine N-acetyltransferase activity / snoRNA localization / leucine zipper domain binding / granular component / U4atac snRNA binding / tRNA acetylation / t-UTP complex / CURI complex / UTP-C complex / Pwp2p-containing subcomplex of 90S preribosome / regulation of stem cell population maintenance / negative regulation of amyloid precursor protein biosynthetic process / box C/D sno(s)RNA binding / histone H2AQ104 methyltransferase activity / Mpp10 complex / rRNA (pseudouridine) methyltransferase activity / endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / dense fibrillar component / pre-snoRNP complex / rRNA modification / regulation of transcription elongation by RNA polymerase II / box C/D sno(s)RNA 3'-end processing / tRNA export from nucleus / endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of centrosome duplication / rRNA methyltransferase activity / histone methyltransferase binding / positive regulation of rRNA processing / box C/D methylation guide snoRNP complex / embryonic cleavage / rRNA base methylation / transcription elongation factor activity / epigenetic programming in the zygotic pronuclei / RNA splicing, via transesterification reactions / blastocyst formation / spindle assembly involved in female meiosis / rRNA primary transcript binding / cilium disassembly / negative regulation of RNA splicing / sno(s)RNA-containing ribonucleoprotein complex / U4 snRNA binding / Cul4-RING E3 ubiquitin ligase complex / telomerase holoenzyme complex / U2-type precatalytic spliceosome / protein localization to nucleolus / box C/D snoRNP assembly / SUMOylation of RNA binding proteins / N-acetyltransferase activity / negative regulation of telomere maintenance via telomerase / neural crest cell differentiation / rRNA modification in the nucleus and cytosol / rRNA methylation / U3 snoRNA binding / Formation of the ternary complex, and subsequently, the 43S complex / response to stimulus / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / ubiquitin ligase inhibitor activity / negative regulation of ubiquitin protein ligase activity / Ribosomal scanning and start codon recognition / precatalytic spliceosome / preribosome, small subunit precursor / Translation initiation complex formation / snoRNA binding / intercellular bridge / NRAGE signals death through JNK / positive regulation of transcription by RNA polymerase I / RNA polymerase II complex binding / protein acetylation / SARS-CoV-1 modulates host translation machinery / Protein hydroxylation / TOR signaling / single fertilization / 90S preribosome / mTORC1-mediated signalling / Association of TriC/CCT with target proteins during biosynthesis / Peptide chain elongation / regulation of mitotic cell cycle / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / TFIID-class transcription factor complex binding / blastocyst development / negative regulation of apoptotic signaling pathway / Response of EIF2AK4 (GCN2) to amino acid deficiency / translation regulator activity / SRP-dependent cotranslational protein targeting to membrane / ubiquitin-like ligase-substrate adaptor activity / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Viral mRNA Translation / chromosome, centromeric region / decidualization Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.51 Å | |||||||||
Authors | Vanden Broeck A / Singh S / Klinge S | |||||||||
Funding support | United States, 2 items
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Citation | Journal: Science / Year: 2021 Title: Nucleolar maturation of the human small subunit processome. Authors: Sameer Singh / Arnaud Vanden Broeck / Linamarie Miller / Malik Chaker-Margot / Sebastian Klinge / Abstract: The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps. We report the high-resolution ...The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps. We report the high-resolution cryo–electron microscopy structures of maturing human small subunit (SSU) processomes at resolutions of 2.7 to 3.9 angstroms. These structures reveal the molecular mechanisms that enable crucial progressions during SSU processome maturation. RNA folding states within these particles are communicated to and coordinated with key enzymes that drive irreversible steps such as targeted exosome-mediated RNA degradation, protein-guided site-specific endonucleolytic RNA cleavage, and tightly controlled RNA unwinding. These conserved mechanisms highlight the SSU processome’s impressive structural plasticity, which endows this 4.5-megadalton nucleolar assembly with the distinctive ability to mature the small ribosomal subunit from within. | |||||||||
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_23939.map.gz | 50.7 MB | EMDB map data format | |
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Header (meta data) | emd-23939-v30.xml emd-23939.xml | 18.1 KB 18.1 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_23939_fsc.xml | 19.8 KB | Display | FSC data file |
Images | emd_23939.png | 147.7 KB | ||
Masks | emd_23939_msk_1.map | 669.9 MB | Mask map | |
Others | emd_23939_additional_1.map.gz emd_23939_half_map_1.map.gz emd_23939_half_map_2.map.gz | 625.2 MB 541.8 MB 541.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-23939 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-23939 | HTTPS FTP |
-Related structure data
Related structure data | 7mq8C 7mq9C 7mqaC 7mqjC C: citing same article (ref.) |
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Similar structure data | |
EM raw data | EMPIAR-10781 (Title: Nucleolar maturation of the human small subunit processome Data size: 74.6 TB Data #1: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 1 [micrographs - multiframe] Data #2: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 2 [micrographs - multiframe] Data #3: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 3 [micrographs - multiframe] Data #4: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 4 [micrographs - multiframe] Data #5: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 5 [micrographs - multiframe] Data #6: Unaligned multi-frame micrograph movies of human SSU processomes - Dataset 6 [micrographs - multiframe] Data #7: Aligned and averaged micrographs of human SSU processomes - Dataset 1 [micrographs - single frame] Data #8: Aligned and averaged micrographs of human SSU processomes - Dataset 2 [micrographs - single frame] Data #9: Aligned and averaged micrographs of human SSU processomes - Dataset 3 [micrographs - single frame] Data #10: Aligned and averaged micrographs of human SSU processomes - Dataset 4 [micrographs - single frame] Data #11: Aligned and averaged micrographs of human SSU processomes - Dataset 5 [micrographs - single frame] Data #12: Aligned and averaged micrographs of human SSU processomes - Dataset 6 [micrographs - single frame]) |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_23939.map.gz / Format: CCP4 / Size: 669.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Main map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_23939_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_23939_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Half-Map1
File | emd_23939_half_map_1.map | ||||||||||||
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Annotation | Half-Map1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-Map2
File | emd_23939_half_map_2.map | ||||||||||||
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Annotation | Half-Map2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human SSU processome, state pre-A1
Entire | Name: Human SSU processome, state pre-A1 |
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Components |
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-Supramolecule #1: Human SSU processome, state pre-A1
Supramolecule | Name: Human SSU processome, state pre-A1 / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 5 MDa |
-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 | Model: Quantifoil R2/2 / Material: GOLD / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 3.0 nm / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 0.01 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 0.7000000000000001 µm |
Specialist optics | Energy filter - Slit width: 20 eV |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 84904 / Average electron dose: 58.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Space: REAL |
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