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994 a.a.
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(+ 6 more)
139 a.a.
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* Residue conservation analysis
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PDB id:
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Contractile protein/transport protein
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Title:
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3-d structure of myosin-v inhibited state
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Structure:
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Myosin-5a. Chain: a, m. Fragment: residues 1-1080. Synonym: myosin va, dilute myosin heavy chain, non-muscle, myosin heavy chain p190, myosin-v. Engineered: yes. Calmodulin. Chain: b, c, d, e, f, g, n, o, p, q, r, s. Synonym: cam.
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9. Mus musculus. House mouse. Organism_taxid: 10090.
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Authors:
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J.Liu,D.W.Taylor,E.B.Krementsova,K.M.Trybus,K.A.Taylor
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Key ref:
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J.Liu
et al.
(2006).
Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography.
Nature,
442,
208-211.
PubMed id:
DOI:
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Date:
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03-Mar-06
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Release date:
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25-Apr-06
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PROCHECK
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Headers
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References
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DOI no:
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Nature
442:208-211
(2006)
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PubMed id:
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Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography.
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J.Liu,
D.W.Taylor,
E.B.Krementsova,
K.M.Trybus,
K.A.Taylor.
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ABSTRACT
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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.
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Selected figure(s)
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Figure 2.
Figure 2: Molecular arrangement within the 'flower' motif. a,
At the top is an opaque surface rendering viewed from the
solvent phase; at the bottom is a translucent surface view with
the myoV atomic model rendered in space filling. The colour
scheme for the bottom molecule is as follows: red and magenta,
motor domains; green, light chains; blue, heavy chain component
of the lever arm; cyan, S2 domain; yellow, cargo-binding domain
density envelope; grey, adjacent molecules. b, c,
Higher-magnification views showing the motor domain fit into the
density envelope. b, View from the solvent phase; c, view from
the monolayer side.
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Figure 4.
Figure 4: Orientation of the myoV-inhibited structure on
F-actin. F-actin strands rendered light blue and grey. Actin
docking is based on ref. 30. a, Panel shows F-actin can bind
only one myoV head at a time. The unbound head extends up
towards the viewer. b, Same view direction as a but with the
second head docked. c, High-magnification gallery of actin-bound
myoV molecules. In some the S2 domain can be seen between the
two heads. Drying in negative stain would flatten the structure
onto a plane, which may account for some of the differences
between the models and the micrographs.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2006,
442,
208-211)
copyright 2006.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.L.Lawson,
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EMDataBank.org: unified data resource for CryoEM.
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Nucleic Acids Res,
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C.Veigel,
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PDB code:
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C.F.Song,
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Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: evidence for stator ring curvature and rotor/C-ring assembly flexion.
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J Bacteriol,
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W.Hwang,
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Cell Biochem Biophys,
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Calcium-activated Myosin V closes the Drosophila pupil.
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Curr Biol,
18,
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E.C.Casavola,
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A.Di Pentima,
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Ypt32p and Mlc1p bind within the vesicle binding region of the class V myosin Myo2p globular tail domain.
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F.Buss,
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Biochem Biophys Res Commun,
369,
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F.Ye,
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Integrin alpha IIb beta 3 in a membrane environment remains the same height after Mn2+ activation when observed by cryoelectron tomography.
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J Mol Biol,
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J Exp Bot,
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J.L.Ross,
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(2008).
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Curr Opin Cell Biol,
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J.W.Hammond,
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Traffic,
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K.M.Trybus
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Myosin V from head to tail.
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M.C.Pranchevicius,
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H.C.Ishikawa-Ankerhold,
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C.T.dos Santos,
M.C.Barreira,
E.M.Espreafico,
and
R.E.Larson
(2008).
Myosin Va phosphorylated on Ser1650 is found in nuclear speckles and redistributes to nucleoli upon inhibition of transcription.
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Cell Motil Cytoskeleton,
65,
441-456.
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N.M.Kad,
K.M.Trybus,
and
D.M.Warshaw
(2008).
Load and Pi control flux through the branched kinetic cycle of myosin V.
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J Biol Chem,
283,
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R.D.Eppinga,
I.F.Peng,
J.L.Lin,
C.F.Wu,
and
J.J.Lin
(2008).
Opposite effects of overexpressed myosin Va or heavy meromyosin Va on vesicle distribution, cytoskeleton organization, and cell motility in nonmuscle cells.
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Cell Motil Cytoskeleton,
65,
197-215.
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X.D.Li,
H.S.Jung,
Q.Wang,
R.Ikebe,
R.Craig,
and
M.Ikebe
(2008).
The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va.
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Proc Natl Acad Sci U S A,
105,
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Y.Fujiyoshi,
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Electron crystallography of proteins in membranes.
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Curr Opin Struct Biol,
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D.W.Provance,
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X.D.Li,
I.G.Davison,
M.Ikebe,
J.A.Mercer,
J.A.Kauer,
and
M.D.Ehlers
(2008).
Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity.
|
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Cell,
135,
535-548.
|
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A.Heuck,
T.G.Du,
S.Jellbauer,
K.Richter,
C.Kruse,
S.Jaklin,
M.Müller,
J.Buchner,
R.P.Jansen,
and
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(2007).
Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes.
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Proc Natl Acad Sci U S A,
104,
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D.Cai,
A.D.Hoppe,
J.A.Swanson,
and
K.J.Verhey
(2007).
Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells.
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J Cell Biol,
176,
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A.Cheng,
and
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(2007).
On the freezing and identification of lipid monolayer 2-D arrays for cryoelectron microscopy.
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J Struct Biol,
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H.L.Sweeney,
and
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What can myosin VI do in cells?
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Curr Opin Cell Biol,
19,
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J.A.Hammer,
and
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(2007).
Slip sliding away with myosin V.
|
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Proc Natl Acad Sci U S A,
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and
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(2007).
The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery.
|
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J Mol Biol,
372,
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PDB code:
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J.E.Norville,
D.F.Kelly,
T.F.Knight,
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and
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7A projection map of the S-layer protein sbpA obtained with trehalose-embedded monolayer crystals.
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Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells.
|
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J Cell Biol,
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|
| |
Proc Natl Acad Sci U S A,
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|
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| |
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| |
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PDB code:
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A.Houdusse,
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Proc Natl Acad Sci U S A,
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PDB code:
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A.O.Olivares,
W.Chang,
M.S.Mooseker,
D.D.Hackney,
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| |
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|
| |
J Biol Chem,
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|
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(2006).
Regulation of myosin V processivity by calcium at the single molecule level.
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J Biol Chem,
281,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
