› 6oay

Electron Microscopy
3.3Å resolution

Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state

Released:
DOI: 10.2210/pdb6oay/pdb
PDB entry 6oay coloured by chain, front view.
PDB entry 6oay coloured by chain, side view.
PDB entry 6oay coloured by chain, top view.
Source organisms:
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-20005

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-159083 (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: 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:
Alpha-S1-casein Chain: P
Molecule details ›
Chain: P
Length: 26 amino acids
Theoretical weight: 2.23 KDa
Source organism: Bos taurus

Ligands and Environments

2 bound ligands:
Ligand AGS 7 x AGS
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-20005
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Protein aggregation in bacteria.
Schramm et al. (2020)
14 more

4 mentions without citation

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