› 5kne

Electron Microscopy
5.64Å resolution

CryoEM Reconstruction of Hsp104 Hexamer

Released:
DOI: 10.2210/pdb5kne/pdb
PDB entry 5kne coloured by chain, front view.
PDB entry 5kne coloured by chain, side view.
PDB entry 5kne coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.
Yokom AL, Gates SN, Jackrel ME, Mack KL, Su M, Shorter J, Southworth DR
Nat Struct Mol Biol 23 830-7 (2016)
PMID: 27478928
Related structures: EMD-8267

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-152028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 104 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 852 amino acids
Theoretical weight: 95.97 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P31539 (Residues: 6-857; Coverage: 94%)
Gene names: HSP104, L0948, YLL026W
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ANP 11 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 5.64Å
Relevant EMDB volumes: EMD-8267
Expression system: Escherichia coli

Quick links

Citations

20 review citations

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

18 mentions without citation

A History of Molecular Chaperone Structures in the Protein Data Bank.
Bascos et al. (2019)
17 more