› 1gml

X-ray diffraction
2.2Å resolution

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

Released:
DOI: 10.2210/pdb1gml/pdb
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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
Molecule details ›
Chains: A, B, C, D
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 GOL 4 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P1
Unit cell:
a: 51.74Å b: 65.02Å c: 65.47Å
α: 89.97° β: 103.95° γ: 90.35°
R-values:
R R work R free
0.203 0.203 0.234
Expression system: Escherichia coli

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Citations

15 review citations

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

3 mentions without citation

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Cong et al. (2010)
2 more

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