› 1gn1

X-ray diffraction
2.8Å resolution

crystal structure of the mouse CCT gamma apical domain (monoclinic)

Released:
DOI: 10.2210/pdb1gn1/pdb
PDB entry 1gn1 coloured by chain, front view.
PDB entry 1gn1 coloured by chain, side view.
PDB entry 1gn1 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin.
Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH
J Mol Biol 318 1367-79 (2002)
PMID: 12083524

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T-complex protein 1 subunit gamma Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 178 amino acids
Theoretical weight: 20.64 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80318 (Residues: 209-380; Coverage: 32%)
Gene names: Cct3, Cctg
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains: GroEL

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 60.244Å b: 234.229Å c: 62.703Å
α: 90° β: 114.7° γ: 90°
R-values:
R R work R free
0.238 0.238 0.285
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Two families of chaperonin: physiology and mechanism.
Horwich et al. (2007)
13 more

1 mention without citation

The role of the molecular chaperone CCT in protein folding and mediation of cytoskeleton-associated processes: implications for cancer cell biology.
Vallin et al. (2019)