› 4d2x

Electron Microscopy
20Å resolution

Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)

Released:
DOI: 10.2210/pdb4d2x/pdb
PDB entry 4d2x coloured by chain, front view.
PDB entry 4d2x coloured by chain, side view.
PDB entry 4d2x coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.
Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR
Elife 3 e02481 (2014)
PMID: 24843029
Related structures: EMD-2559

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpB Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 858 amino acids
Theoretical weight: 96.84 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P63284 (Residues: 1-857; Coverage: 100%)
Gene names: JW2573, b2592, clpB, htpM
Sequence domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 126 x MSE

Experiments and Validation Details

Entry percentile scores
Resolution: 20Å
Relevant EMDB volumes: EMD-2559
Expression system: Escherichia coli

Quick links

Citations

19 review citations

How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.
Clerico et al. (2015)
18 more

4 mentions without citation

Structural mechanisms of chaperone mediated protein disaggregation.
Sousa R. (2014)
3 more