› 6og2

Electron Microscopy
4.1Å resolution

Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, post-state

Released:
DOI: 10.2210/pdb6og2/pdb
PDB entry 6og2 coloured by chain, front view.
PDB entry 6og2 coloured by chain, side view.
PDB entry 6og2 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.
Rizo AN, Lin J, Gates SN, Tse E, Bart SM, Castellano LM, DiMaio F, Shorter J, Southworth DR
Nat Commun 10 2393 (2019)
PMID: 31160557
Related structures: EMD-20050

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpB Chains: A, F
Molecule details ›
Chains: A, F
Length: 867 amino acids
Theoretical weight: 97.02 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P63284 (Residues: 1-857; Coverage: 100%)
Gene names: JW2573, b2592, clpB, htpM
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 3 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.1Å
Relevant EMDB volumes: EMD-20050
Expression system: Escherichia coli

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Citations

17 review citations

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Puchades et al. (2020)
16 more