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PDBsum entry 5i0i
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Motor protein
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PDB id
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5i0i
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Contents |
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784 a.a.
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145 a.a.
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43 a.a.
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59 a.a.
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PDB id:
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| Name: |
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Motor protein
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Title:
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Crystal structure of myosin x motor domain with 2iq motifs in pre- powerstroke state
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Structure:
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Unconventional myosin-x. Chain: a, b. Synonym: unconventional myosin-10. Engineered: yes. Calmodulin. Chain: c. Synonym: cam. Engineered: yes. Calmodulin.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: myo10, kiaa0799. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469. Gene: calm1, calm, cam, cam1, calm2, cam2, camb, calm3, calml2, cam3, camc, camiii. Expression_system_taxid: 10469
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Resolution:
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3.15Å
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R-factor:
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0.193
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R-free:
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0.219
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Authors:
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T.Isabet,H.L.Sweeney,A.Houdusse
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Key ref:
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V.Ropars
et al.
(2016).
The myosin X motor is optimized for movement on actin bundles.
Nat Commun,
7,
12456.
PubMed id:
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Date:
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04-Feb-16
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Release date:
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07-Sep-16
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PROCHECK
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Headers
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References
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Q9HD67
(MYO10_HUMAN) -
Unconventional myosin-X from Homo sapiens
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Seq:
Struc:
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2058 a.a.
784 a.a.
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P0DP23
(CALM1_HUMAN) -
Calmodulin-1 from Homo sapiens
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Seq:
Struc:
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149 a.a.
145 a.a.
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Nat Commun
7:12456
(2016)
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PubMed id:
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The myosin X motor is optimized for movement on actin bundles.
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V.Ropars,
Z.Yang,
T.Isabet,
F.Blanc,
K.Zhou,
T.Lin,
X.Liu,
P.Hissier,
F.Samazan,
B.Amigues,
E.D.Yang,
H.Park,
O.Pylypenko,
M.Cecchini,
C.V.Sindelar,
H.L.Sweeney,
A.Houdusse.
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ABSTRACT
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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.
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Links
