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Open data
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Basic information
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Title | Cryo-em structure of the Nup98 fibril polymorph 3 | |||||||||
![]() | Cryo-em structure of the Nup98 fibril polymorph 3 | |||||||||
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Function / homology | ![]() telomere tethering at nuclear periphery / nuclear pore organization / nuclear pore outer ring / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / ![]() | |||||||||
![]() | Ibanez de Opakua A / Geraets JA / Frieg B / Dienemann C / Savastano A / Rankovic M / Cima-Omori M-S / Schroeder GF / Zweckstetter M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular interactions of FG nucleoporin repeats at high resolution. Authors: Alain Ibáñez de Opakua / James A Geraets / Benedikt Frieg / Christian Dienemann / Adriana Savastano / Marija Rankovic / Maria-Sol Cima-Omori / Gunnar F Schröder / Markus Zweckstetter / ![]() Abstract: Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear ...Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities. | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 5.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.5 KB 15.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.9 KB | Display | ![]() |
Images | ![]() | 63.8 KB | ||
Others | ![]() ![]() | 46.2 MB 46.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7q66MC ![]() 7q64C ![]() 7q65C ![]() 7q67C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Annotation | Cryo-em structure of the Nup98 fibril polymorph 3 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
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
-Half map: Cryo-em structure of the Nup98 fibril polymorph 3, half map 1
File | emd_13853_half_map_1.map | ||||||||||||
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Annotation | Cryo-em structure of the Nup98 fibril polymorph 3, half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Cryo-em structure of the Nup98 fibril polymorph 3, half map 2
File | emd_13853_half_map_2.map | ||||||||||||
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Annotation | Cryo-em structure of the Nup98 fibril polymorph 3, half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Cryo-em structure of the Nup98 fibril polymorph 3
Entire | Name: Cryo-em structure of the Nup98 fibril polymorph 3 |
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Components |
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-Supramolecule #1: Cryo-em structure of the Nup98 fibril polymorph 3
Supramolecule | Name: Cryo-em structure of the Nup98 fibril polymorph 3 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: The Nup98 polymorph 3 fibril is formed by two protofilaments, consisting of Nup98 monomers. |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Nuclear pore complex protein Nup98
Macromolecule | Name: Nuclear pore complex protein Nup98 / type: protein_or_peptide / ID: 1 / Number of copies: 22 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 4.005211 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: TGTANTLFGT ASTGTSLFSS QNNAFAQNKP TGFGNFGTST |
-Experimental details
-Structure determination
Method | ![]() |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7 / Component: | ||||
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / 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 (6k x 4k) / Number real images: 4180 / Average exposure time: 2.557 sec. / Average electron dose: 41.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |