+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-8244 | |||||||||
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Title | Rigor myosin X co-complexed with an actin filament | |||||||||
Map data | Rigor myosin X co-complexed with an actin filament | |||||||||
Sample |
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Keywords | myosin molecular motors cytoskeletal motility / MOTOR PROTEIN | |||||||||
Function / homology | Function and homology information plus-end directed microfilament motor activity / Netrin-1 signaling / positive regulation of cell-cell adhesion / filopodium tip / cytoskeleton-dependent intracellular transport / regulation of filopodium assembly / filopodium membrane / myosin complex / cytoskeletal motor activator activity / microfilament motor activity ...plus-end directed microfilament motor activity / Netrin-1 signaling / positive regulation of cell-cell adhesion / filopodium tip / cytoskeleton-dependent intracellular transport / regulation of filopodium assembly / filopodium membrane / myosin complex / cytoskeletal motor activator activity / microfilament motor activity / spectrin binding / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / filamentous actin / actin filament bundle / phosphatidylinositol-3,4,5-trisphosphate binding / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / ruffle / actin filament polymerization / filopodium / actin filament / FCGR3A-mediated phagocytosis / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Regulation of actin dynamics for phagocytic cup formation / calcium-dependent protein binding / actin filament binding / lamellipodium / regulation of cell shape / cell cortex / cell body / calmodulin binding / hydrolase activity / neuron projection / protein domain specific binding / neuronal cell body / calcium ion binding / positive regulation of gene expression / nucleolus / magnesium ion binding / signal transduction / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / Oryctolagus cuniculus (rabbit) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 9.1 Å | |||||||||
Authors | Sindelar CV / Houdusse A | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2016 Title: The myosin X motor is optimized for movement on actin bundles. Authors: Virginie Ropars / Zhaohui Yang / Tatiana Isabet / Florian Blanc / Kaifeng Zhou / Tianming Lin / Xiaoyan Liu / Pascale Hissier / Frédéric Samazan / Béatrice Amigues / Eric D Yang / Hyokeun ...Authors: Virginie Ropars / Zhaohui Yang / Tatiana Isabet / Florian Blanc / Kaifeng Zhou / Tianming Lin / Xiaoyan Liu / Pascale Hissier / Frédéric Samazan / Béatrice Amigues / Eric D Yang / Hyokeun Park / Olena Pylypenko / Marco Cecchini / Charles V Sindelar / H Lee Sweeney / Anne Houdusse / Abstract: Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and ...Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_8244.map.gz | 7.5 MB | EMDB map data format | |
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Header (meta data) | emd-8244-v30.xml emd-8244.xml | 18.4 KB 18.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_8244_fsc.xml | 5.4 KB | Display | FSC data file |
Images | emd_8244.png | 217.3 KB | ||
Masks | emd_8244_msk_1.map | 8 MB | Mask map | |
Filedesc metadata | emd-8244.cif.gz | 6.5 KB | ||
Others | emd_8244_half_map_1.map.gz emd_8244_half_map_2.map.gz | 7.4 MB 7.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8244 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8244 | HTTPS FTP |
-Validation report
Summary document | emd_8244_validation.pdf.gz | 1012 KB | Display | EMDB validaton report |
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Full document | emd_8244_full_validation.pdf.gz | 1011.6 KB | Display | |
Data in XML | emd_8244_validation.xml.gz | 10.4 KB | Display | |
Data in CIF | emd_8244_validation.cif.gz | 13.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8244 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8244 | HTTPS FTP |
-Related structure data
Related structure data | 5kg8MC 5hmoC 5hmpC 5i0hC 5i0iC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_8244.map.gz / Format: CCP4 / Size: 8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Rigor myosin X co-complexed with an actin filament | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.868 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_8244_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Rigor myosin X co-complexed with an actin filament, half map #1
File | emd_8244_half_map_1.map | ||||||||||||
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Annotation | Rigor myosin X co-complexed with an actin filament, half map #1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Rigor myosin X co-complexed with an actin filament, half map #2
File | emd_8244_half_map_2.map | ||||||||||||
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Annotation | Rigor myosin X co-complexed with an actin filament, half map #2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Actin filament decorated by the myosin X motor domain
Entire | Name: Actin filament decorated by the myosin X motor domain |
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Components |
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-Supramolecule #1: Actin filament decorated by the myosin X motor domain
Supramolecule | Name: Actin filament decorated by the myosin X motor domain / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Macromolecule #1: Unconventional myosin-X
Macromolecule | Name: Unconventional myosin-X / 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: 85.083086 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: NFFTEGTRVW LRENGQHFPS TVNSCAEGIV VFRTDYGQVF TYKQSTITHQ KVTAMHPTNE EGVDDMASLT ELHGGSIMYN LFQRYKRNQ IYTYIGSILA SVNPYQPIAG LYEPATMEQY SRRHLGELPP HIFAIANECY RCLWKRHDNQ CILISGESGA G KTESTKLI ...String: NFFTEGTRVW LRENGQHFPS TVNSCAEGIV VFRTDYGQVF TYKQSTITHQ KVTAMHPTNE EGVDDMASLT ELHGGSIMYN LFQRYKRNQ IYTYIGSILA SVNPYQPIAG LYEPATMEQY SRRHLGELPP HIFAIANECY RCLWKRHDNQ CILISGESGA G KTESTKLI LKFLSVISQQ SLELSLKEKT SCVERAILES SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI VD YLLEKNR VVRQNPGERN YHIFYALLAG LEHEEREEFY LSTPENYHYL NQSGCVEDKT ISDQESFREV ITAMDVMQFS KEE VREVSR LLAGILHLGN IEFITAGGAQ VSFKTALGRS AELLGLDPTQ LTDALTQRSM FLRGEEILTP LNVQQAVDSR DSLA MALYA CCFEWVIKKI NSRIKGNEDF KSIGILDIFG FENFEVNHFE QFNINYANEK LQEYFNKHIF SLEQLEYSRE GLVWE DIDW IDNGECLDLI EKKLGLLALI NEESHFPQAT DSTLLEKLHS QHANNHFYVK PRVAVNNFGV KHYAGEVQYD VRGILE KNR DTFRDDLLNL LRESRFDFIY DLFEHVSSRN NQDAAAAAAA ARRPTVSSQF KDSLHSLMAT LSSSNPFFVR CIKPNMQ KM PDQFDQAVVL NQLRYSGMLE TVRIRKAGYA VRRPFQDFYK RYKVLMRNLA LPEDVRGKCT SLLQLYDASN SEWQLGKT K VFLRESLEQK LEKRREEE UniProtKB: Unconventional myosin-X |
-Macromolecule #2: Actin, alpha skeletal muscle
Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Oryctolagus cuniculus (rabbit) |
Molecular weight | Theoretical: 41.827609 KDa |
Sequence | String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IECGIITNWD DMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV T HNVPIYEG ...String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IECGIITNWD DMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV T HNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN VMSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ITKQEYDEAG PSIVHRKCF UniProtKB: Actin, alpha skeletal muscle |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Concentration | 1.7 mg/mL |
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Buffer | pH: 6.8 / Component - Concentration: 5.0 mM / Component - Name: MOPS |
Grid | Model: Quantifoil / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY |
Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER |
-Electron microscopy
Microscope | FEI TECNAI F20 |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 2 / Number real images: 154 / Average exposure time: 13.0 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 5.251 µm / Calibrated defocus min: 1.438 µm / Calibrated magnification: 26780 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal defocus max: 5.0 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |