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- EMDB-43370: Fascin crosslinked F-actin hexagonal bundle element (460 Angstrom box) -
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Open data
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Basic information
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Title | Fascin crosslinked F-actin hexagonal bundle element (460 Angstrom box) | |||||||||
![]() | Local filtered map | |||||||||
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![]() | Cytoskeleton / F-actin crosslinker / F-actin bundle / STRUCTURAL PROTEIN | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.7 Å | |||||||||
![]() | Gong R / Reynolds MJ / Alushin GM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Fascin structural plasticity mediates flexible actin bundle construction. Authors: Rui Gong / Matthew J Reynolds / Keith R Carney / Keith Hamilton / Tamara C Bidone / Gregory M Alushin / ![]() Abstract: Fascin cross-links actin filaments (F-actin) into bundles that support tubular membrane protrusions including filopodia and stereocilia. Fascin dysregulation drives aberrant cell migration during ...Fascin cross-links actin filaments (F-actin) into bundles that support tubular membrane protrusions including filopodia and stereocilia. Fascin dysregulation drives aberrant cell migration during metastasis, and fascin inhibitors are under development as cancer therapeutics. Here, we use cryo-EM, cryo-electron tomography coupled with custom denoising and computational modeling to probe human fascin-1's F-actin cross-linking mechanisms across spatial scales. Our fascin cross-bridge structure reveals an asymmetric F-actin binding conformation that is allosterically blocked by the inhibitor G2. Reconstructions of seven-filament hexagonal bundle elements, variability analysis and simulations show how structural plasticity enables fascin to bridge varied interfilament orientations, accommodating mismatches between F-actin's helical symmetry and bundle hexagonal packing. Tomography of many-filament bundles and modeling uncover geometric rules underlying emergent fascin binding patterns, as well as the accumulation of unfavorable cross-links that limit bundle size. Collectively, this work shows how fascin harnesses fine-tuned nanoscale structural dynamics to build and regulate micron-scale F-actin bundles. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 198.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.6 KB 16.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16 KB | Display | ![]() |
Images | ![]() | 100 KB | ||
Masks | ![]() | 343 MB | ![]() | |
Filedesc metadata | ![]() | 5.5 KB | ||
Others | ![]() ![]() ![]() | 273.6 MB 274 MB 274 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 23.5 KB | Display | |
Data in CIF | ![]() | 31.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Local filtered map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.03 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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Density Histograms |
-Additional map: Unfiltered reconstruction
File | emd_43370_additional_1.map | ||||||||||||
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Annotation | Unfiltered reconstruction | ||||||||||||
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Density Histograms |
-Half map: Half map 2
File | emd_43370_half_map_1.map | ||||||||||||
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Annotation | Half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 1
File | emd_43370_half_map_2.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Fascin crosslinked F-actin
Entire | Name: Fascin crosslinked F-actin |
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Components |
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-Supramolecule #1: Fascin crosslinked F-actin
Supramolecule | Name: Fascin crosslinked F-actin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 5.4 kDa/nm |
-Macromolecule #1: Fascin 1
Macromolecule | Name: Fascin 1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GPLGSMTANG TAEAVQIQFG LINCGNKYLT AEAFGFKVNA SASSLKKKQI WTLEQPPDEA GSAAVCLRSH LGRYLAADKD GNVTCEREVP GPDCRFLIVA HDDGRWSLQS EAHRRYFGGT EDRLSCFAQT VSPAEKWSVH IAMHPQVNIY SVTRKRYAHL SARPADEIAV ...String: GPLGSMTANG TAEAVQIQFG LINCGNKYLT AEAFGFKVNA SASSLKKKQI WTLEQPPDEA GSAAVCLRSH LGRYLAADKD GNVTCEREVP GPDCRFLIVA HDDGRWSLQS EAHRRYFGGT EDRLSCFAQT VSPAEKWSVH IAMHPQVNIY SVTRKRYAHL SARPADEIAV DRDVPWGVDS LITLAFQDQR YSVQTADHRF LRHDGRLVAR PEPATGYTLE FRSGKVAFRD CEGRYLAPSG PSGTLKAGKA TKVGKDELFA LEQSCAQVVL QAANERNVST RQGMDLSANQ DEETDQETFQ LEIDRDTKKC AFRTHTGKYW TLTATGGVQS TASSKNASCY FDIEWRDRRI TLRASNGKFV TSKKNGQLAA SVETAGDSEL FLMKLINRPI IVFRGEHGFI GCRKVTGTLD ANRSSYDVFQ LEFNDGAYNI KDSTGKYWTV GSDSAVTSSG DTPVDFFFEF CDYNKVAIKV GGRYLKGDHA GVLKASAETV DPASLWEY |
-Macromolecule #2: Alpha actin
Macromolecule | Name: Alpha actin / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: DETTALVCDN GSGLVKAGFA GDDAPRAVFP SIVGRPRHQG VMVGMGQKDS YVGDEAQSKR GILTLKYPIE (HIC)GIITNWDDM EKIWHHTFYN ELRVAPEEHP TLLTEAPLNP KANREKMTQI MFETFNVPAM YVAIQAVLSL YASGRTTGIV LDSGDGVTHN VPIYEGYALP ...String: DETTALVCDN GSGLVKAGFA GDDAPRAVFP SIVGRPRHQG VMVGMGQKDS YVGDEAQSKR GILTLKYPIE (HIC)GIITNWDDM EKIWHHTFYN ELRVAPEEHP TLLTEAPLNP KANREKMTQI MFETFNVPAM YVAIQAVLSL YASGRTTGIV LDSGDGVTHN VPIYEGYALP HAIMRLDLAG RDLTDYLMKI LTERGYSFVT TAEREIVRDI KEKLCYVALD FENEMATAAS SSSLEKSYEL PDGQVITIGN ERFRCPETLF QPSFIGMESA GIHETTYNSI MKCDIDIRKD LYANNVMSGG TTMYPGIADR MQKEITALAP STMKIKIIAP PERKYSVWIG GSILASLSTF QQMWITKQEY DEAGPSIVHR KCF |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 61.26 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |