› 4i2z

X-ray diffraction
2.9Å resolution

Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide

Released:
DOI: 10.2210/pdb4i2z/pdb
PDB entry 4i2z coloured by chain, front view.
PDB entry 4i2z coloured by chain, side view.
PDB entry 4i2z 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-124527 (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 90 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.18 KDa
Source organism: Caenorhabditis elegans
Expression system: Not provided
UniProt:
  • Canonical: Q18688 (Residues: 693-702; Coverage: 1%)
Gene names: C47E8.5, daf-21

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6122
Unit cell:
a: 86.633Å b: 86.633Å c: 815.015Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.256
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

9 review citations

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

9 mentions without citation

The UNC-45 myosin chaperone: from worms to flies to vertebrates.
Lee et al. (2014)
8 more