› 6w6g

Electron Microscopy
3.1Å resolution

The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate

Released:
DOI: 10.2210/pdb6w6g/pdb
PDB entry 6w6g coloured by chain, front view.
PDB entry 6w6g coloured by chain, side view.
PDB entry 6w6g coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Yin Y, Feng X, Yu H, Fay A, Kovach A, Glickman MS, Li H
Cell Rep 35 109166 (2021)
PMID: 34038719
Related structures: EMD-21554

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161964 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein ClpB Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 848 amino acids
Theoretical weight: 92.69 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPD1 (Residues: 1-848; Coverage: 100%)
Gene names: MTV036.19c, Rv0384c, clpB
Sequence domains:
Substrate Chain: N
Molecule details ›
Chain: N
Length: 33 amino acids
Theoretical weight: 2.83 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand AGS 10 x AGS
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-21554
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future.
Burley et al. (2022)
1 more

1 mention without citation

Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Yin et al. (2021)