|Entry||Database: EMDB / ID: EMD-1201|
|Title||Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography.|
|Map data||This the 3-D average map of myosin-V in "off" state|
|Function / homology|
Function and homology information
Cam-PDE 1 activation / Glycogen breakdown (glycogenolysis) / CaMK IV-mediated phosphorylation of CREB / Activation of RAC1 downstream of NMDARs / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / CLEC7A (Dectin-1) induces NFAT activation / Activation of Ca-permeable Kainate Receptor / Sodium/Calcium exchangers / Reduction of cytosolic Ca++ levels / Calcineurin activates NFAT ...Cam-PDE 1 activation / Glycogen breakdown (glycogenolysis) / CaMK IV-mediated phosphorylation of CREB / Activation of RAC1 downstream of NMDARs / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / CLEC7A (Dectin-1) induces NFAT activation / Activation of Ca-permeable Kainate Receptor / Sodium/Calcium exchangers / Reduction of cytosolic Ca++ levels / Calcineurin activates NFAT / Synthesis of IP3 and IP4 in the cytosol / RHO GTPases activate PAKs / Inactivation, recovery and regulation of the phototransduction cascade / Calmodulin induced events / eNOS activation / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Ion transport by P-type ATPases / Phase 0 - rapid depolarisation / Unblocking of NMDA receptors, glutamate binding and activation / Protein methylation / RAF activation / Ca2+ pathway / RAS processing / negative regulation of calcium ion import across plasma membrane / VEGFR2 mediated vascular permeability / protein serine/threonine phosphatase complex / Smooth Muscle Contraction / Extra-nuclear estrogen signaling / RHO GTPases activate IQGAPs / negative regulation of calcium ion transmembrane transporter activity / minus-end directed microfilament motor activity / RAF/MAP kinase cascade / positive regulation of voltage-gated calcium channel activity / calcineurin complex / insulin-responsive compartment / PKA activation / negative regulation of voltage-gated calcium channel activity / Platelet degranulation / Stimuli-sensing channels / positive regulation of calcium ion import across plasma membrane / DAPK1-calmodulin complex / regulation of response to tumor cell / positive regulation of autophagic cell death / Ion homeostasis / FCERI mediated Ca+2 mobilization / positive regulation of calcineurin-NFAT signaling cascade / establishment of protein localization to mitochondrial membrane / vesicle transport along actin filament / type 3 metabotropic glutamate receptor binding / regulation of synaptic vesicle endocytosis / organelle localization by membrane tethering / myosin complex / response to corticosterone / autophagosome membrane docking / microfilament motor activity / mitochondrion-endoplasmic reticulum membrane tethering / regulation of cardiac muscle cell action potential / negative regulation of high voltage-gated calcium channel activity / N-terminal myristoylation domain binding / negative regulation of calcium ion export across plasma membrane / positive regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / adenylate cyclase binding / sperm midpiece / filamentous actin / positive regulation of cyclic-nucleotide phosphodiesterase activity / nitric-oxide synthase binding / detection of calcium ion / catalytic complex / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction / calcium channel inhibitor activity / positive regulation of phosphoprotein phosphatase activity / activation of adenylate cyclase activity / potassium ion transmembrane transport / adenylate cyclase activator activity / regulation of calcium-mediated signaling / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / phosphatidylinositol 3-kinase binding / titin binding / positive regulation of protein dephosphorylation / voltage-gated potassium channel complex / sarcomere / calcium channel complex / regulation of ryanodine-sensitive calcium-release channel activity / response to amphetamine / regulation of heart rate / mitochondrial membrane / enzyme regulator activity / nitric-oxide synthase regulator activity / actin filament organization / vesicle-mediated transport / calcium-mediated signaling / protein localization to plasma membrane / regulation of cytokinesis / regulation of synaptic vesicle exocytosis / synaptic vesicle membrane / positive regulation of DNA binding / response to calcium ion / spindle microtubule
Similarity search - Function
Myosin 5a, cargo-binding domain / Class V myosin, motor domain / DIL / DIL domain / Dilute domain / Dilute domain profile. / IQ calmodulin-binding motif / Myosin N-terminal SH3-like domain profile. / Myosin, N-terminal, SH3-like / Short calmodulin-binding motif containing conserved Ile and Gln residues. ...Myosin 5a, cargo-binding domain / Class V myosin, motor domain / DIL / DIL domain / Dilute domain / Dilute domain profile. / IQ calmodulin-binding motif / Myosin N-terminal SH3-like domain profile. / Myosin, N-terminal, SH3-like / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin motor domain profile. / Myosin head, motor domain / Myosin. Large ATPases. / Myosin head (motor domain) / IQ motif profile. / IQ motif, EF-hand binding site / Kinesin motor domain superfamily / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Calmodulin-1 / Calmodulin-2 / Unconventional myosin-Va
Similarity search - Component
|Biological species||Mus musculus (house mouse)|
|Method||subtomogram averaging / cryo EM / negative staining / Resolution: 24.0 Å|
|Authors||Liu J / Taylor DW / Krementsova EB / Trybus KM / Taylor KA|
|Citation||Journal: Nature / Year: 2006|
Title: Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography.
Authors: Jun Liu / Dianne W Taylor / Elena B Krementsova / Kathleen M Trybus / Kenneth A Taylor /
Abstract: Unconventional myosin V (myoV) is an actin-based molecular motor that has a key function in organelle and mRNA transport, as well as in membrane trafficking. MyoV was the first member of the myosin ...Unconventional myosin V (myoV) is an actin-based molecular motor that has a key function in organelle and mRNA transport, as well as in membrane trafficking. MyoV was the first member of the myosin superfamily shown to be processive, meaning that a single motor protein can 'walk' hand-over-hand along an actin filament for many steps before detaching. Full-length myoV has a low actin-activated MgATPase activity at low [Ca2+], whereas expressed constructs lacking the cargo-binding domain have a high activity regardless of [Ca2+] (refs 5-7). Hydrodynamic data and electron micrographs indicate that the active state is extended, whereas the inactive state is compact. Here we show the first three-dimensional structure of the myoV inactive state. Each myoV molecule consists of two heads that contain an amino-terminal motor domain followed by a lever arm that binds six calmodulins. The heads are followed by a coiled-coil dimerization domain (S2) and a carboxy-terminal globular cargo-binding domain. In the inactive structure, bending of myoV at the head-S2 junction places the cargo-binding domain near the motor domain's ATP-binding pocket, indicating that ATPase inhibition might occur through decreased rates of nucleotide exchange. The actin-binding interfaces are unobstructed, and the lever arm is oriented in a position typical of strong actin-binding states. This structure indicates that motor recycling after cargo delivery might occur through transport on actively treadmilling actin filaments rather than by diffusion.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_1201.map.gz / Format: CCP4 / Size: 7.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Annotation||This the 3-D average map of myosin-V in "off" state|
|Projections & slices|
Images are generated by Spider.
generated in cubic-lattice coordinate
|Voxel size||X=Y=Z: 5.56 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire : MYOSIN V
|Entire||Name: MYOSIN V|
-Supramolecule #1000: MYOSIN V
|Supramolecule||Name: MYOSIN V / type: sample / ID: 1000 / Number unique components: 1|
|Molecular weight||Experimental: 400 KDa / Theoretical: 400 KDa|
-Macromolecule #1: Myosin-V
|Macromolecule||Name: Myosin-V / type: protein_or_peptide / ID: 1 / Name.synonym: MYOV / Details: expressed full lengh myosin-V / Number of copies: 2 / Oligomeric state: Dimer / Recombinant expression: Yes|
|Source (natural)||Organism: Mus musculus (house mouse) / synonym: mouse|
|Molecular weight||Experimental: 400 KDa / Theoretical: 400 KDa|
|Recombinant expression||Organism: Sf9 cells|
|Method||negative staining, cryo EM|
|Aggregation state||2D array|
|Buffer||Details: 20 mM Na2HPO4, 80-100 mM NaCl, 2 mM MgCl2, 1 mM ADP, 1 mM EGTA|
Details: MyoV 2-D arrays were recovered from the lipid monolayer
|Grid||Details: 200 mesh copper grids covered with a reticulated carbon film.|
|Vitrification||Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 277 K / Instrument: HOMEMADE PLUNGER / Details: Vitrification instrument: in house plunger / Method: Blot for 3 seconds before plunging|
|Details||crystals grown on a lipid-monolayer|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.0 mm / Nominal defocus max: 12.0 µm / Nominal defocus min: 4.0 µm / Nominal magnification: 24000|
|Sample stage||Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN / Tilt series - Axis1 - Min angle: 0 ° / Tilt series - Axis1 - Max angle: 70 °|
|Temperature||Average: 103 K|
|Date||Feb 1, 2004|
|Image recording||Category: CCD / Film or detector model: TVIPS TEMCAM-F224 (2k x 2k) / Digitization - Sampling interval: 24 µm / Number real images: 360 / Average electron dose: 30 e/Å2|
|Crystal parameters||Unit cell - A: 653 Å / Unit cell - B: 653 Å / Unit cell - γ: 120 ° / Unit cell - α: 90.0 ° / Unit cell - β: 90.0 ° / Plane group: P 6|
|CTF correction||Details: focus gradient correction|
|Final reconstruction||Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 24.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: protomo|
-Atomic model buiding 1
|Software||Name: Situs and NMFF|
|Details||Protocol: Rigid body and Normal Mode Flexible. Start with Rigid body docking by using SITUS and refine with NMFF|
|Refinement||Space: REAL / Protocol: FLEXIBLE FIT / Target criteria: Correlation|
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