|Entry||Database: PDB / ID: 5kg8|
|Title||Rigor myosin X co-complexed with an actin filament|
|Keywords||MOTOR PROTEIN / myosin molecular motors cytoskeletal motility|
|Function / homology|
Function and homology information
plus-end directed microfilament motor activity / filopodium tip / cytoskeleton-dependent intracellular transport / regulation of filopodium assembly / filopodium membrane / microfilament motor activity => GO:0000146 / positive regulation of microfilament motor activity => GO:0120081 / myosin complex / mesenchyme migration / tropomyosin binding ...plus-end directed microfilament motor activity / filopodium tip / cytoskeleton-dependent intracellular transport / regulation of filopodium assembly / filopodium membrane / microfilament motor activity => GO:0000146 / positive regulation of microfilament motor activity => GO:0120081 / myosin complex / mesenchyme migration / tropomyosin binding / myosin heavy chain binding / troponin I binding / spectrin binding / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle / filamentous actin / phosphatidylinositol-3,4,5-trisphosphate binding / actin monomer binding / actin filament bundle assembly / skeletal muscle fiber development / skeletal muscle myofibril / stress fiber / titin binding / actin filament polymerization / ruffle / filopodium / actin filament / cell cortex / cell body / calcium-dependent protein binding / Fc-gamma receptor signaling pathway involved in phagocytosis / actin filament binding / lamellipodium / regulation of cell shape / calmodulin binding / protein domain specific binding / nucleolus / positive regulation of gene expression / calcium ion binding / magnesium ion binding / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm
Actin / FERM superfamily, second domain / Actin family / Pleckstrin homology domain / Myosin head, motor domain / MyTH4 domain / FERM domain / Ras-associating (RA) domain / IQ motif, EF-hand binding site / FERM/acyl-CoA-binding protein superfamily ...Actin / FERM superfamily, second domain / Actin family / Pleckstrin homology domain / Myosin head, motor domain / MyTH4 domain / FERM domain / Ras-associating (RA) domain / IQ motif, EF-hand binding site / FERM/acyl-CoA-binding protein superfamily / FERM central domain / Band 4.1 domain / Actin/actin-like conserved site / PH-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase / Unconventional myosin-X, coiled coil domain / Actin, conserved site / Class X myosin, motor domain / Myosin X, N-terminal SH3 domain / Myosin X N-terminal SH3 domain / Myosin head (motor domain) / ATPase, nucleotide binding domain / Myosin X, FERM domain C-lobe / MyTH4 domain superfamily / Kinesin motor domain superfamily
Actin, alpha skeletal muscle / Unconventional myosin-X
|Biological species||Homo sapiens (human)|
Oryctolagus cuniculus (rabbit)
|Method||ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 9.1 Å|
|Authors||Sindelar, C.V. / Houdusse, A. / Sweeney, L.|
|Funding support|| United States, 1items |
|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.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Unconventional myosin-X
B: Actin, alpha skeletal muscle
C: Actin, alpha skeletal muscle
D: Actin, alpha skeletal muscle
|#1: Protein|| |
Mass: 85083.086 Da / Num. of mol.: 1 / Fragment: motor domain (UNP residues 3-741)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MYO10, KIAA0799 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HD67
Mass: 41827.609 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / References: UniProt: P68135
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction|
|Component||Name: Actin filament decorated by the myosin X motor domain / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1-#2 / Source: MULTIPLE SOURCES|
|Buffer solution||pH: 6.8|
|Buffer component||Conc.: 5 mM / Name: MOPS|
|Specimen||Conc.: 1.7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil|
|Vitrification||Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Microscopy||Model: FEI TECNAI F20|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy / Calibrated magnification: 26780 X / Nominal defocus max: 5000 nm / Nominal defocus min: 1000 nm / Calibrated defocus min: 1438 nm / Calibrated defocus max: 5251 nm / Cs: 2 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE|
|Specimen holder||Cryogen: NITROGEN|
Model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER
|Image recording||Average exposure time: 13 sec. / Electron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 154|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: 167.1 ° / Axial rise/subunit: 27.44 Å / Axial symmetry: C1 / Details: Not directly applicable to the modeled coordinates|
|3D reconstruction||Resolution: 9.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 57927 / Algorithm: FOURIER SPACE|
Details: Symmetry was not applied in this reconstruction. The provided symmetry parameters are nominal, and were not actually used.
Num. of class averages: 1 / Symmetry type: HELICAL
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