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Contents |
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772 a.a.
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136 a.a.
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151 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Contractile protein
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Title:
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Scallop myosin s1 complexed with mgadp:vanadate-transition state
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Structure:
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Myosin head. Chain: a, b. Fragment: heavy chain. Myosin head. Chain: y, w. Fragment: regulatory light chain. Myosin head. Chain: z, x. Fragment: essential light chain
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Source:
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Argopecten irradians. Organism_taxid: 31199. Tissue: skeletal muscle. Tissue: skeletal muscle
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Biol. unit:
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Trimer (from
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Resolution:
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4.20Å
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R-factor:
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0.394
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R-free:
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0.400
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Authors:
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A.Houdusse,A.G.Szent-Gyorgyi,C.Cohen
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Key ref:
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A.Houdusse
et al.
(2000).
Three conformational states of scallop myosin S1.
Proc Natl Acad Sci U S A,
97,
11238-11243.
PubMed id:
DOI:
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Date:
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19-Nov-99
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Release date:
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25-Oct-00
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PROCHECK
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Headers
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References
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P24733
(MYS_ARGIR) -
Myosin heavy chain, striated muscle from Argopecten irradians
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Seq:
Struc:
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1938 a.a.
772 a.a.
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Enzyme class:
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Chains A, Y, Z, B, W, X:
E.C.?
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DOI no:
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Proc Natl Acad Sci U S A
97:11238-11243
(2000)
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PubMed id:
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Three conformational states of scallop myosin S1.
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A.Houdusse,
A.G.Szent-Gyorgyi,
C.Cohen.
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ABSTRACT
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We have determined the structure of the intact scallop myosin head, containing
both the motor domain and the lever arm, in the nucleotide-free state and in the
presence of MgADP.V04, corresponding to the transition state. These two new
structures, together with the previously determined structure of scallop S1
complexed with MgADP (which we interpret as a detached ATP state), reveal three
conformations of an intact S1 obtained from a single isoform. These studies,
together with new crystallization results, show how the conformation of the
motor depends on the nucleotide content of the active site. The resolution of
the two new structures ( approximately 4 A) is sufficient to establish the
relative positions of the subdomains and the overall conformation of the joints
within the motor domain as well as the position of the lever arm. Comparison of
available crystal structures from different myosin isoforms and truncated
constructs in either the nucleotide-free or transition states indicates that the
major features within the motor domain are relatively invariant in both these
states. In contrast, the position of the lever arm varies significantly between
different isoforms. These results indicate that the heavy-chain helix is pliant
at the junction between the converter and the lever arm and that factors other
than the precise position of the converter can influence the position of the
lever arm. It is possible that this pliant junction in the myosin head
contributes to the compliance known to be present in the crossbridge.
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Selected figure(s)
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Figure 2.
Fig. 2. (A) Ribbon diagrams of the nucleotide-free
scallop S1 structure (Lower) and of scallop S1-VO[4] (Upper)
oriented such that the lower 50-kDa subdomains of these two
structures superimpose. An arrow indicates the approximate
direction of the actin filament axis relative to this subdomain,
deduced from an electron microscope study of S1-decorated actin
(16). The position of the ELC in the scallop nucleotide-free
structure is very close to that found in the electron-microscope
maps of actin decorated with vertebrate smooth muscle myosin S1
under rigor conditions (16). No data are available to indicate
how S1 binds to actin in the prepower stroke state; for
illustrative purposes only, we have chosen to orient this
structure by assuming that the interactions with the lower
50-kDa subdomain would be conserved. The lever arm is positioned
at  90° and
25° to the actin filament axis in the transition-state and
near-rigor structures, respectively. (Note that for measuring
angles, the lever-arm position is taken as a straight line drawn
from the N-terminal side of the lever-arm helix to the sharp
bend near the C terminus.) (B) Schematic drawings of the
transition-state and the near-rigor conformations of scallop
myosin from an interpretation of the structures seen in A. The
rotation of the converter (green)/relay (yellow) module during
the power stroke is amplified by the lever arm (scallop blue
helix, light chains omitted for clarity). The direction of the
movement of the subdomains in the transition between the two
states is indicated with black arrows. Although the subdomains
of the MD are similar in different isoforms, differences are
seen in the lever-arm position. To illustrate this point, the
position of the lever arm found in smooth muscle MDE (purple
helix, Upper) and that of chicken striated muscle myosin S1
(purple helix, Lower) is compared with the positions found for
scallop myosin in the transition state and near-rigor state,
respectively. Differences in the bending of the heavy-chain
helix at the junction between the converter and the lever arm
result in markedly different orientations for the lever arm of
these structures representing the same state. (C) Schematic
drawing of an orthogonal view of the structures seen in A. In
this orientation, the actin filament axis is approximately
perpendicular to the page, and one can thus estimate the
azimuthal component of the movement of the lever arm. This
component is very small in the case of scallop. In contrast,
bending of the heavy-chain helix at the pliant region in smooth
MDE in the transition-state conformation could lead to a large
azimuthal component during the power-stroke in this myosin.
Comparison of the transition-state and near-rigor conformations
in this view reveals changes in the position of the upper and
lower 50-kDa subdomains related to differences in both the
conformation of switch II and the actin-binding site.
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Figure 3.
Fig. 3. Ribbon diagrams of the nucleotide-free scallop S1
structure in near-rigor, transition, and detached states,
oriented such that the lower 50-kDa subdomains of these three
structures superimpose. An arrow indicates the approximate
direction of the actin filament axis relative to this subdomain,
deduced from electron microscope studies (13, 16). The light
chains bound to the heavy-chain helix of the lever arm in these
three structures are omitted for clarity. Large differences are
found in the position of the converter and result from
relatively small rearrangements of the other three subdomains of
the MD (not shown). In the three scallop S1 structures, the
heavy-chain helix is straight at the junction between the
converter and the lever arm, and the interactions at the
interface between the converter and the ELC seem to be conserved.
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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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|
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J.H.Brown,
V.S.Kumar,
E.O'Neall-Hennessey,
L.Reshetnikova,
H.Robinson,
M.Nguyen-McCarty,
A.G.Szent-Györgyi,
and
C.Cohen
(2011).
Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.
|
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Proc Natl Acad Sci U S A,
108,
114-119.
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PDB code:
|
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|
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|
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O.Pylypenko,
and
A.M.Houdusse
(2011).
Essential "ankle" in the myosin lever arm.
|
| |
Proc Natl Acad Sci U S A,
108,
5-6.
|
|
|
|
|
|
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A.Málnási-Csizmadia,
and
M.Kovács
(2010).
Emerging complex pathways of the actomyosin powerstroke.
|
| |
Trends Biochem Sci,
35,
684-690.
|
|
|
|
|
|
|
C.D.Williams,
M.Regnier,
and
T.L.Daniel
(2010).
Axial and radial forces of cross-bridges depend on lattice spacing.
|
| |
PLoS Comput Biol,
6,
e1001018.
|
|
|
|
|
|
|
G.Offer,
and
K.W.Ranatunga
(2010).
Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.
|
| |
J Muscle Res Cell Motil,
31,
245-265.
|
|
|
|
|
|
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H.L.Sweeney,
and
A.Houdusse
(2010).
Structural and functional insights into the Myosin motor mechanism.
|
| |
Annu Rev Biophys,
39,
539-557.
|
|
|
|
|
|
|
R.Tehver,
and
D.Thirumalai
(2010).
Rigor to post-rigor transition in myosin V: link between the dynamics and the supporting architecture.
|
| |
Structure,
18,
471-481.
|
|
|
|
|
|
|
S.Wu,
J.Liu,
M.C.Reedy,
R.T.Tregear,
H.Winkler,
C.Franzini-Armstrong,
H.Sasaki,
C.Lucaveche,
Y.E.Goldman,
M.K.Reedy,
and
K.A.Taylor
(2010).
Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions.
|
| |
PLoS One,
5,
0.
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|
PDB codes:
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D.D.Thomas,
D.Kast,
and
V.L.Korman
(2009).
Site-directed spectroscopic probes of actomyosin structural dynamics.
|
| |
Annu Rev Biophys,
38,
347-369.
|
|
|
|
|
|
|
D.R.Weiss,
and
M.Levitt
(2009).
Can morphing methods predict intermediate structures?
|
| |
J Mol Biol,
385,
665-674.
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S.Wu,
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M.C.Reedy,
H.Winkler,
M.K.Reedy,
and
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(2009).
Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle.
|
| |
J Struct Biol,
168,
485-502.
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|
|
|
|
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S.Xu,
H.D.White,
G.W.Offer,
and
L.C.Yu
(2009).
Stabilization of helical order in the thick filaments by blebbistatin: further evidence of coexisting multiple conformations of myosin.
|
| |
Biophys J,
96,
3673-3681.
|
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|
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Y.Xu,
and
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(2009).
Comprehensive physical mechanism of two-headed biomotor myosin V.
|
| |
J Chem Phys,
131,
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A.C.Knowles,
R.E.Ferguson,
B.D.Brandmeier,
Y.B.Sun,
D.R.Trentham,
and
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(2008).
Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscle.
|
| |
Biophys J,
95,
3882-3891.
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|
|
A.Pecci,
E.Panza,
N.Pujol-Moix,
C.Klersy,
F.Di Bari,
V.Bozzi,
P.Gresele,
S.Lethagen,
F.Fabris,
C.Dufour,
A.Granata,
M.Doubek,
C.Pecoraro,
P.A.Koivisto,
P.G.Heller,
A.Iolascon,
P.Alvisi,
D.Schwabe,
E.De Candia,
B.Rocca,
U.Russo,
U.Ramenghi,
P.Noris,
M.Seri,
C.L.Balduini,
and
A.Savoia
(2008).
Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations predicts the natural history of MYH9-related disease.
|
| |
Hum Mutat,
29,
409-417.
|
|
|
|
|
|
|
F.Q.Zhao,
R.Padrón,
and
R.Craig
(2008).
Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.
|
| |
Biophys J,
95,
3322-3329.
|
|
|
|
|
|
|
H.S.Jung,
S.A.Burgess,
N.Billington,
M.Colegrave,
H.Patel,
J.M.Chalovich,
P.D.Chantler,
and
P.J.Knight
(2008).
Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution.
|
| |
Proc Natl Acad Sci U S A,
105,
6022-6026.
|
|
|
|
|
|
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H.S.Jung,
S.Komatsu,
M.Ikebe,
and
R.Craig
(2008).
Head-head and head-tail interaction: a general mechanism for switching off myosin II activity in cells.
|
| |
Mol Biol Cell,
19,
3234-3242.
|
|
|
|
|
|
|
I.Aprodu,
A.Redaelli,
and
M.Soncini
(2008).
Actomyosin interaction: mechanical and energetic properties in different nucleotide binding States.
|
| |
Int J Mol Sci,
9,
1927-1943.
|
|
|
|
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|
J.H.Brown,
Y.Yang,
L.Reshetnikova,
S.Gourinath,
D.Süveges,
J.Kardos,
F.Hóbor,
R.Reutzel,
L.Nyitray,
and
C.Cohen
(2008).
An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins.
|
| |
J Mol Biol,
375,
1434-1443.
|
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|
PDB codes:
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J.Ménétrey,
P.Llinas,
J.Cicolari,
G.Squires,
X.Liu,
A.Li,
H.L.Sweeney,
and
A.Houdusse
(2008).
The post-rigor structure of myosin VI and implications for the recovery stroke.
|
| |
EMBO J,
27,
244-252.
|
|
|
PDB codes:
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J.P.Schmidt,
S.L.Delp,
M.A.Sherman,
C.A.Taylor,
V.S.Pande,
and
R.B.Altman
(2008).
The Simbios National Center: Systems Biology in Motion.
|
| |
Proc IEEE Inst Electr Electron Eng,
96,
1266-1280.
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W.Wriggers,
A.Pinto,
F.Bártoli,
L.Salazar,
F.Q.Zhao,
R.Craig,
and
R.Padrón
(2008).
Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.
|
| |
J Mol Biol,
384,
780-797.
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PDB code:
|
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|
|
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|
|
M.Cecchini,
A.Houdusse,
and
M.Karplus
(2008).
Allosteric communication in myosin V: from small conformational changes to large directed movements.
|
| |
PLoS Comput Biol,
4,
e1000129.
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|
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|
|
M.J.Harris,
and
H.J.Woo
(2008).
Energetics of subdomain movements and fluorescence probe solvation environment change in ATP-bound myosin.
|
| |
Eur Biophys J,
38,
1.
|
|
|
|
|
|
|
N.A.Koubassova,
S.Y.Bershitsky,
M.A.Ferenczi,
and
A.K.Tsaturyan
(2008).
Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.
|
| |
Biophys J,
95,
2880-2894.
|
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S.L.Hooper,
K.H.Hobbs,
and
J.B.Thuma
(2008).
Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.
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| |
Prog Neurobiol,
86,
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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.
|
| |
Proc Natl Acad Sci U S A,
105,
1140-1145.
|
|
|
|
|
|
|
E.Brunello,
M.Reconditi,
R.Elangovan,
M.Linari,
Y.B.Sun,
T.Narayanan,
P.Panine,
G.Piazzesi,
M.Irving,
and
V.Lombardi
(2007).
Skeletal muscle resists stretch by rapid binding of the second motor domain of myosin to actin.
|
| |
Proc Natl Acad Sci U S A,
104,
20114-20119.
|
|
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|
|
|
|
H.Park,
A.Li,
L.Q.Chen,
A.Houdusse,
P.R.Selvin,
and
H.L.Sweeney
(2007).
The unique insert at the end of the myosin VI motor is the sole determinant of directionality.
|
| |
Proc Natl Acad Sci U S A,
104,
778-783.
|
|
|
|
|
|
|
J.Borejdo,
P.Muthu,
J.Talent,
I.Akopova,
and
T.P.Burghardt
(2007).
Rotation of actin monomers during isometric contraction of skeletal muscle.
|
| |
J Biomed Opt,
12,
014013.
|
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J.Ménétrey,
P.Llinas,
M.Mukherjea,
H.L.Sweeney,
and
A.Houdusse
(2007).
The structural basis for the large powerstroke of myosin VI.
|
| |
Cell,
131,
300-308.
|
|
|
PDB code:
|
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|
|
|
|
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L.Shakirova,
V.Mikhailova,
E.Siletskaya,
V.P.Timofeev,
and
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(2007).
Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1.
|
| |
J Muscle Res Cell Motil,
28,
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N.M.Kad,
J.B.Patlak,
P.M.Fagnant,
K.M.Trybus,
and
D.M.Warshaw
(2007).
Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.
|
| |
Biophys J,
92,
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|
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|
S.Tang,
J.C.Liao,
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J.A.Spudich,
and
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(2007).
Predicting allosteric communication in myosin via a pathway of conserved residues.
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| |
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H.W.Schroeder,
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K.Homma,
M.Ikebe,
and
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(2007).
Myosin VI walks "wiggly" on actin with large and variable tilting.
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| |
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|
| |
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|
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PDB codes:
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|
A.Ganoth,
R.Friedman,
E.Nachliel,
and
M.Gutman
(2006).
A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides.
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Brownian molecular motors driven by rotation-translation coupling.
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Phys Rev E Stat Nonlin Soft Matter Phys,
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(2006).
Strain-dependent kinetics of the myosin working stroke, and how they could be probed with optical-trap experiments.
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| |
Biophys J,
91,
3359-3369.
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J.H.Collins
(2006).
Myoinformatics report: myosin regulatory light chain paralogs in the human genome.
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| |
J Muscle Res Cell Motil,
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J.Sleep,
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and
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(2006).
Reconciling the working strokes of a single head of skeletal muscle myosin estimated from laser-trap experiments and crystal structures.
|
| |
Proc Natl Acad Sci U S A,
103,
1278-1282.
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|
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J.A.Hammer,
J.R.Sellers,
and
P.J.Knight
(2006).
The cargo-binding domain regulates structure and activity of myosin 5.
|
| |
Nature,
442,
212-215.
|
|
|
|
|
|
|
P.Petrone,
and
V.S.Pande
(2006).
Can conformational change be described by only a few normal modes?
|
| |
Biophys J,
90,
1583-1593.
|
|
|
|
|
|
|
S.Xu,
J.Gu,
B.Belknap,
H.White,
and
L.C.Yu
(2006).
Structural characterization of the binding of Myosin*ADP*Pi to actin in permeabilized rabbit psoas muscle.
|
| |
Biophys J,
91,
3370-3382.
|
|
|
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|
V.Azzu,
D.Yadin,
H.Patel,
F.Fraternali,
P.D.Chantler,
and
J.E.Molloy
(2006).
Calcium regulates scallop muscle by changing myosin flexibility.
|
| |
Eur Biophys J,
35,
302-312.
|
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|
W.Zheng,
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
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