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PDBsum entry 4r8g
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Protein binding/calcium-binding protein
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PDB id
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4r8g
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Contents |
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324 a.a.
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136 a.a.
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144 a.a.
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PDB id:
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Protein binding/calcium-binding protein
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Title:
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Crystal structure of myosin-1c tail in complex with calmodulin
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Structure:
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Unconventional myosin-ic. Chain: e. Fragment: unp residues 733-1063. Synonym: myosin i beta, mmi-beta, mmib. Engineered: yes. Calmodulin. Chain: b, a, h. Synonym: cam. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: myo1c. Expressed in: escherichia coli. Expression_system_taxid: 562. Xenopus laevis. Clawed frog,common platanna,platanna. Organism_taxid: 8355.
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Resolution:
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3.50Å
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R-factor:
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0.246
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R-free:
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0.304
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Authors:
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Q.Lu,J.Li,F.Ye,M.Zhang
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Key ref:
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Q.Lu
et al.
(2015).
Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.
Nat Struct Mol Biol,
22,
81-88.
PubMed id:
DOI:
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Date:
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02-Sep-14
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Release date:
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03-Dec-14
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PROCHECK
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Headers
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References
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Q9WTI7
(MYO1C_MOUSE) -
Unconventional myosin-Ic from Mus musculus
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Seq: Struc:
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1063 a.a.
324 a.a.
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DOI no:
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Nat Struct Mol Biol
22:81-88
(2015)
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PubMed id:
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Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.
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Q.Lu,
J.Li,
F.Ye,
M.Zhang.
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ABSTRACT
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Class I myosins can sense cellular mechanical forces and function as
tension-sensitive anchors or transporters. How mechanical load is transduced
from the membrane-binding tail to the force-generating head in myosin-1 is
unknown. Here we determined the crystal structure of the entire tail of mouse
myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable
monomer conformation suited for force transduction. The lever-arm helix and the
C-terminal extended PH domain of the motor are coupled by a stable post-IQ
domain bound to calmodulin in a highly unusual mode. Ca(2+) binding to
calmodulin induces major conformational changes in both IQ motifs and the
post-IQ domain and increases flexibility of the myosin-1c tail. Our study
provides a structural blueprint for the neck and tail domains of myosin-1 and
expands the target binding modes of the master Ca(2+)-signal regulator
calmodulin.
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');
}
}
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