› 4i2w

X-ray diffraction
3.6Å resolution

Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp70 peptide

Released:
DOI: 10.2210/pdb4i2w/pdb
PDB entry 4i2w coloured by chain, front view.
PDB entry 4i2w coloured by chain, side view.
PDB entry 4i2w coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.
Gazda L, Pokrzywa W, Hellerschmied D, Löwe T, Forné I, Mueller-Planitz F, Hoppe T, Clausen T
Cell 152 183-95 (2013)
PMID: 23332754

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124526 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
UNC-45/Cro1/She4 central domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 961 amino acids
Theoretical weight: 108.93 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G5EG62 (Residues: 1-961; Coverage: 100%)
Gene names: CELE_F30H5.1, F30H5.1, unc-45
Sequence domains: Myosin-binding striated muscle assembly central
Structure domains:
Heat shock protein hsp-1 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 987 Da
Source organism: Caenorhabditis elegans
Expression system: Not provided
UniProt:
  • Canonical: P09446 (Residues: 631-640; Coverage: 2%)
Gene names: F26D10.3, hsp-1, hsp70a

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 29 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P6122
Unit cell:
a: 86.276Å b: 86.276Å c: 808.978Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.234 0.284
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

SMYD proteins: key regulators in skeletal and cardiac muscle development and function.
Du et al. (2014)
10 more

1 mention without citation

Domain architecture of BAF250a reveals the ARID and ARM-repeat domains with implication in function and assembly of the BAF remodeling complex.
Sandhya et al. (2018)