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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | U2 snRNP after ATP-dependent remodelling | |||||||||
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Function / homology | ![]() U11/U12 snRNP / B-WICH complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Tholen J / Galej WP | |||||||||
Funding support | European Union, 1 items
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![]() | ![]() Title: Structural basis of branch site recognition by the human spliceosome. Authors: Jonas Tholen / Michal Razew / Felix Weis / Wojciech P Galej / ![]() ![]() Abstract: Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and ...Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and unambiguous intron recognition cannot be achieved solely through a base-pairing mechanism. We isolated human 17 U2 snRNP and reconstituted in vitro its adenosine 5´-triphosphate (ATP)–dependent remodeling and binding to the pre–messenger RNA substrate. We determined a series of high-resolution (2.0 to 2.2 angstrom) structures providing snapshots of the BS selection process. The substrate-bound U2 snRNP shows that SF3B6 stabilizes the BS:U2 snRNA duplex, which could aid binding of introns with poor sequence complementarity. ATP-dependent remodeling uncoupled from substrate binding captures U2 snRNA in a conformation that competes with BS recognition, providing a selection mechanism based on branch helix stability. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 809.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 31.5 KB 31.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 22.5 KB | Display | ![]() |
Images | ![]() | 97.3 KB | ||
Masks | ![]() | 1000 MB | ![]() | |
Others | ![]() ![]() ![]() | 935.7 MB 815.4 MB 818 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7q4pMC ![]() 7q3lC ![]() 7q4oC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
EM raw data | ![]() Data size: 1.5 TB Data #1: Unaligned multi-frame micrographs of the U2 snRNP after ATP-dependent remodeling [micrographs - multiframe] Data #2: Final polished particles of the U2 snRNP after ATP-dependent remodeling [picked particles - single frame - processed]) |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.64 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: Map postprocessed in relion with -37 B-factor.
File | emd_13812_additional_1.map | ||||||||||||
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Annotation | Map postprocessed in relion with -37 B-factor. | ||||||||||||
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-Half map: #2
File | emd_13812_half_map_1.map | ||||||||||||
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-Half map: #1
File | emd_13812_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Remodelled U2 snRNP
+Supramolecule #1: Remodelled U2 snRNP
+Macromolecule #1: Splicing factor 3A subunit 2
+Macromolecule #3: Splicing factor 3A subunit 3
+Macromolecule #4: Splicing factor 3B subunit 1
+Macromolecule #5: Splicing factor 3B subunit 2
+Macromolecule #6: Splicing factor 3B subunit 3
+Macromolecule #7: Splicing factor 3B subunit 5
+Macromolecule #8: PHD finger-like domain-containing protein 5A
+Macromolecule #2: U2 snRNA
+Macromolecule #9: ZINC ION
+Macromolecule #10: water
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Concentration | 0.3 mg/mL | ||||||||||||
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Buffer | pH: 7.9 Component:
Details: Sample after desalting may have also contained up to 5% glycerol. | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD![]() |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 15531 / Average exposure time: 1.0 sec. / Average electron dose: 53.45 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |