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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-6701 | |||||||||
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| Title | 3D cryo-EM reconstruction of Microtubule-WHAMM complex | |||||||||
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Keywords | microtubule / helical reconstruction / STRUCTURAL PROTEIN | |||||||||
| Function / homology | Function and homology informationplasma membrane tubulation / Arp2/3 complex-mediated actin nucleation / Arp2/3 complex binding / positive regulation of actin nucleation / focal adhesion assembly / RHOD GTPase cycle / lamellipodium assembly / endoplasmic reticulum to Golgi vesicle-mediated transport / endoplasmic reticulum-Golgi intermediate compartment membrane / cytoplasmic vesicle membrane ...plasma membrane tubulation / Arp2/3 complex-mediated actin nucleation / Arp2/3 complex binding / positive regulation of actin nucleation / focal adhesion assembly / RHOD GTPase cycle / lamellipodium assembly / endoplasmic reticulum to Golgi vesicle-mediated transport / endoplasmic reticulum-Golgi intermediate compartment membrane / cytoplasmic vesicle membrane / actin filament organization / small GTPase binding / actin binding / microtubule binding / microtubule / Golgi membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
Authors | Liu T / Wang HW | |||||||||
Citation | Journal: J Mol Biol / Year: 2017Title: Structural Insights of WHAMM's Interaction with Microtubules by Cryo-EM. Authors: Tianyang Liu / Anbang Dai / Yong Cao / Rui Zhang / Meng-Qiu Dong / Hong-Wei Wang / ![]() Abstract: WASP homolog associated with actin, membranes, and microtubules (WHAMM) is a vertebrate protein functioning in membrane tubulation for intracellular membrane trafficking and specific organelle ...WASP homolog associated with actin, membranes, and microtubules (WHAMM) is a vertebrate protein functioning in membrane tubulation for intracellular membrane trafficking and specific organelle formation. Composed of multiple domains, WHAMM can bind to membrane and microtubule (MT) and promote actin polymerization nucleation. Previous work revealed that WHAMM's activity to promote actin nucleation is repressed upon binding to MTs. Here, we discovered that WHAMM interacts with αβ-tubulin through a small peptide motif within its MT-binding domain. We reconstructed a high-resolution structure of WHAMM's MT-binding motif (MBM) assembling around MTs using cryo-electron microscopy and verified it with chemical cross-linking and mass spectrometry analysis. We also detected a conformational switch of this motif between the non-MT-bound state and the MT-bound state. These discoveries provide new insights into the mechanism by which WHAMM coordinates actin and MT networks, the two major cytoskeletal systems involved in membrane trafficking and membrane remodeling. | |||||||||
| History |
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_6701.map.gz | 141.8 MB | EMDB map data format | |
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| Header (meta data) | emd-6701-v30.xml emd-6701.xml | 8.6 KB 8.6 KB | Display Display | EMDB header |
| Images | emd_6701.png | 298.9 KB | ||
| Filedesc metadata | emd-6701.cif.gz | 4.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6701 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6701 | HTTPS FTP |
-Validation report
| Summary document | emd_6701_validation.pdf.gz | 501.7 KB | Display | EMDB validaton report |
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| Full document | emd_6701_full_validation.pdf.gz | 501.3 KB | Display | |
| Data in XML | emd_6701_validation.xml.gz | 8.3 KB | Display | |
| Data in CIF | emd_6701_validation.cif.gz | 9.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6701 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6701 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5x1gMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_6701.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.306 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Ternary complex of alpha,beta-tubulin dimer with microtubule bind...
| Entire | Name: Ternary complex of alpha,beta-tubulin dimer with microtubule binding motif of WHAMM |
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| Components |
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-Supramolecule #1: Ternary complex of alpha,beta-tubulin dimer with microtubule bind...
| Supramolecule | Name: Ternary complex of alpha,beta-tubulin dimer with microtubule binding motif of WHAMM type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: WASP homolog-associated protein with actin, membranes and microtubules
| Macromolecule | Name: WASP homolog-associated protein with actin, membranes and microtubules type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 4.414182 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: IQMKRDKIKE EEQKKKEWIN QERQKTLQRL RSFK UniProtKB: WASP homolog-associated protein with actin, membranes and microtubules |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 6.8 |
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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: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Applied symmetry - Helical parameters - Δz: 8.6 Å Applied symmetry - Helical parameters - Δ&Phi: -25.762 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 8000 |
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| Startup model | Type of model: OTHER |
| Final angle assignment | Type: NOT APPLICABLE |
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