› 3kfk

X-ray diffraction
6Å resolution

Crystal structures of a group II chaperonin from Methanococcus maripaludis

Released:
DOI: 10.2210/pdb3kfk/pdb
PDB entry 3kfk coloured by chain, front view.
PDB entry 3kfk coloured by chain, side view.
PDB entry 3kfk coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD
J Biol Chem 285 27958-66 (2010)
PMID: 20573955

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 521 amino acids
Theoretical weight: 55.61 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q877G8 (Residues: 1-543; Coverage: 96%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

1 bound ligand:
Ligand AGS 4 x AGS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: I222
Unit cell:
a: 150.533Å b: 209.527Å c: 266.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.241 0.27
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
9 more

5 mentions without citation

Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
Pereira et al. (2010)
4 more