› 6og3

Electron Microscopy
4.1Å resolution

Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer

Released:
DOI: 10.2210/pdb6og3/pdb
PDB entry 6og3 coloured by chain, front view.
PDB entry 6og3 coloured by chain, side view.
PDB entry 6og3 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-20051

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159080 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein ClpB Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 867 amino acids
Theoretical weight: 96.96 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: 9 amino acids
Theoretical weight: 784 Da
Source organism: Bos taurus

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.1Å
Relevant EMDB volumes: EMD-20051
Expression system: Escherichia coli

Quick links

Citations

17 review citations

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

1 mention without citation

Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action.
Weinhäupl et al. (2022)