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PDBsum entry 4r8g

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protein ligands Protein-protein interface(s) links
Protein binding/calcium-binding protein PDB id
4r8g

 

 

 

 

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Contents
Protein chains
324 a.a.
136 a.a.
144 a.a.
Ligands
SO4 ×3
PDB id:
4r8g
Name: Protein binding/calcium-binding protein
Title: Crystal structure of myosin-1c tail in complex with calmodulin
Structure: 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
Source: 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.
Resolution:
3.50Å     R-factor:   0.246     R-free:   0.304
Authors: Q.Lu,J.Li,F.Ye,M.Zhang
Key ref: 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: 25437912 DOI: 10.1038/nsmb.2923
Date:
02-Sep-14     Release date:   03-Dec-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9WTI7  (MYO1C_MOUSE) -  Unconventional myosin-Ic from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1063 a.a.
324 a.a.
Protein chain
Pfam   ArchSchema ?
P0DP33  (CALM1_XENLA) -  Calmodulin-1 from Xenopus laevis
Seq:
Struc:
149 a.a.
136 a.a.
Protein chains
Pfam   ArchSchema ?
P0DP33  (CALM1_XENLA) -  Calmodulin-1 from Xenopus laevis
Seq:
Struc:
149 a.a.
144 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1038/nsmb.2923 Nat Struct Mol Biol 22:81-88 (2015)
PubMed id: 25437912  
 
 
Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.
Q.Lu, J.Li, F.Ye, M.Zhang.
 
  ABSTRACT  
 
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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