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Yorodumi- EMDB-23940: Cryo-EM structure of the human SSU processome, state post-A1 - ra... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-23940 | |||||||||
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Title | Cryo-EM structure of the human SSU processome, state post-A1 - raw maps | |||||||||
Map data | ||||||||||
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 / tRNA N-acetyltransferase activity / tRNA wobble cytosine modification / snoRNA localization / leucine zipper domain binding / granular component ...mRNA N-acetyltransferase activity / negative regulation of superoxide anion generation / preribosome / oocyte growth / nucleologenesis / tRNA N-acetyltransferase activity / tRNA wobble cytosine modification / snoRNA localization / leucine zipper domain binding / granular component / rRNA acetylation involved in maturation of SSU-rRNA / rRNA cytidine N-acetyltransferase activity / tRNA acetylation / Pwp2p-containing subcomplex of 90S preribosome / U4atac snRNP / regulation of stem cell population maintenance / CURI complex / negative regulation of amyloid precursor protein biosynthetic process / histone H2AQ104 methyltransferase activity / t-UTP complex / UTP-C complex / Mpp10 complex / U4atac snRNA binding / rRNA (pseudouridine) methyltransferase activity / rRNA modification / pre-snoRNP complex / endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / box C/D sno(s)RNA binding / box C/D sno(s)RNA 3'-end processing / endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / dense fibrillar component / regulation of centrosome duplication / endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / tRNA export from nucleus / rRNA methyltransferase activity / histone methyltransferase binding / regulation of transcription elongation by RNA polymerase II / positive regulation of rRNA processing / embryonic cleavage / transcription elongation factor activity / rRNA base methylation / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / rRNA primary transcript binding / cilium disassembly / blastocyst formation / negative regulation of RNA splicing / Cul4-RING E3 ubiquitin ligase complex / RNA splicing, via transesterification reactions / sno(s)RNA-containing ribonucleoprotein complex / N-acetyltransferase activity / protein localization to nucleolus / U4 snRNA binding / telomerase holoenzyme complex / box C/D methylation guide snoRNP complex / SUMOylation of RNA binding proteins / U2-type precatalytic spliceosome / neural crest cell differentiation / rRNA methylation / response to stimulus / Formation of the ternary complex, and subsequently, the 43S complex / rRNA modification in the nucleus and cytosol / box C/D snoRNP assembly / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / U3 snoRNA binding / Ribosomal scanning and start codon recognition / negative regulation of ubiquitin protein ligase activity / preribosome, small subunit precursor / Translation initiation complex formation / snoRNA binding / precatalytic spliceosome / intercellular bridge / NRAGE signals death through JNK / positive regulation of transcription by RNA polymerase I / protein acetylation / Protein hydroxylation / RNA polymerase II complex binding / mTORC1-mediated signalling / SARS-CoV-1 modulates host translation machinery / Association of TriC/CCT with target proteins during biosynthesis / Peptide chain elongation / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Selenocysteine synthesis / Formation of a pool of free 40S subunits / ubiquitin ligase inhibitor activity / TFIID-class transcription factor complex binding / Eukaryotic Translation Termination / blastocyst development / negative regulation of apoptotic signaling pathway / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / negative regulation of telomere maintenance via telomerase / chromosome, centromeric region / Viral mRNA Translation / decidualization / ubiquitin-like ligase-substrate adaptor activity / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / TOR signaling Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.65 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_23940.map.gz | 66.5 MB | EMDB map data format | |
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Header (meta data) | emd-23940-v30.xml emd-23940.xml | 18.1 KB 18.1 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_23940_fsc.xml | 19.7 KB | Display | FSC data file |
Images | emd_23940.png | 169.4 KB | ||
Masks | emd_23940_msk_1.map | 669.9 MB | Mask map | |
Others | emd_23940_additional_1.map.gz emd_23940_half_map_1.map.gz emd_23940_half_map_2.map.gz | 627 MB 542 MB 541.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-23940 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-23940 | 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_23940.map.gz / Format: CCP4 / Size: 669.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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_23940_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_23940_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Half-map1
File | emd_23940_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_23940_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 post-A1
Entire | Name: Human SSU processome, state post-A1 |
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Components |
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-Supramolecule #1: Human SSU processome, state post-A1
Supramolecule | Name: Human SSU processome, state post-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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