› 1u2m

X-ray diffraction
2.3Å resolution

Crystal Structure of Skp

Released:
DOI: 10.2210/pdb1u2m/pdb
PDB entry 1u2m coloured by chain, front view.
PDB entry 1u2m coloured by chain, side view.
PDB entry 1u2m coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.
Walton TA, Sousa MC
Mol Cell 15 367-74 (2004)
PMID: 15304217

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein Skp Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 143 amino acids
Theoretical weight: 16.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEU7 (Residues: 21-161; Coverage: 100%)
Gene names: JW0173, b0178, hlpA, ompH, skp
Sequence domains: Outer membrane protein (OmpH-like)
Structure domains: Skp domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P212121
Unit cell:
a: 55.828Å b: 84.19Å c: 160.181Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.259
Expression system: Escherichia coli

Quick links

Citations

45 review citations

Translocation of proteins into mitochondria.
Neupert et al. (2007)
44 more

11 mentions without citation

Transmembrane β-barrels: Evolution, folding and energetics.
Chaturvedi et al. (2017)
10 more