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- EMDB-16836: Structure of the Pol II-SPT6-Elongin complex (structure 1, global map) -
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Open data
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Basic information
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Title | Structure of the Pol II-SPT6-Elongin complex (structure 1, global map) | ||||||||||||
![]() | Global map for Pol II-SPT6-Elongin structure | ||||||||||||
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![]() | Transcription elongation / Elongin / ![]() ![]() | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Chen Y / Kokic G / Dienemann C / Dybkov O / Urlaub H / Cramer P | ||||||||||||
Funding support | European Union, ![]()
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![]() | ![]() Title: Structure of the transcribing RNA polymerase II-Elongin complex. Authors: Ying Chen / Goran Kokic / Christian Dienemann / Olexandr Dybkov / Henning Urlaub / Patrick Cramer / ![]() ![]() Abstract: Elongin is a heterotrimeric elongation factor for RNA polymerase (Pol) II transcription that is conserved among metazoa. Here, we report three cryo-EM structures of human Elongin bound to ...Elongin is a heterotrimeric elongation factor for RNA polymerase (Pol) II transcription that is conserved among metazoa. Here, we report three cryo-EM structures of human Elongin bound to transcribing Pol II. The structures show that Elongin subunit ELOA binds the RPB2 side of Pol II and anchors the ELOB-ELOC subunit heterodimer. ELOA contains a 'latch' that binds between the end of the Pol II bridge helix and funnel helices, thereby inducing a conformational change near the polymerase active center. The latch is required for the elongation-stimulatory activity of Elongin, but not for Pol II binding, indicating that Elongin functions by allosterically regulating the conformational mobility of the polymerase active center. Elongin binding to Pol II is incompatible with association of the super elongation complex, PAF1 complex and RTF1, which also contain an elongation-stimulatory latch element. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 301.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.1 KB 16.1 KB | Display Display | ![]() |
Images | ![]() | 95.2 KB | ||
Masks | ![]() | 325 MB | ![]() | |
Filedesc metadata | ![]() | 4.3 KB | ||
Others | ![]() ![]() | 261.7 MB 261.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Global map for Pol II-SPT6-Elongin structure | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 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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Projections & Slices |
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Density Histograms |
-Half map: half map 1 for generating the global map
File | emd_16836_half_map_1.map | ||||||||||||
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Annotation | half map 1 for generating the global map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 2 for generating the global map
File | emd_16836_half_map_2.map | ||||||||||||
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Annotation | half map 2 for generating the global map | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : The Pol II-SPT6-Elongin transcription elongation complex
Entire | Name: The Pol II-SPT6-Elongin transcription elongation complex |
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Components |
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-Supramolecule #1: The Pol II-SPT6-Elongin transcription elongation complex
Supramolecule | Name: The Pol II-SPT6-Elongin transcription elongation complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#19 Details: The map is generated from a sub-class of a Cryo-EM dataset for the Pol II-SPT6-Elongin complex. |
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Source (natural) | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R3.5/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2.1 |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.09 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.05 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 72087 |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: OTHER |
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