› 3bbu

Electron Microscopy
10Å resolution

The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex

Released:
DOI: 10.2210/pdb3bbu/pdb
PDB entry 3bbu coloured by chain, front view.
PDB entry 3bbu coloured by chain, side view.
PDB entry 3bbu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Recycling of aborted ribosomal 50S subunit-nascent chain-tRNA complexes by the heat shock protein Hsp15.
Jiang L, Schaffitzel C, Bingel-Erlenmeyer R, Ban N, Korber P, Koning RI, de Geus DC, Plaisier JR, Abrahams JP
J Mol Biol 386 1357-67 (2009)
PMID: 19013177
Related structures: EMD-1455

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142277 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 15 Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.9 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0ACG8 (Residues: 5-108; Coverage: 78%)
Gene names: JW3363, b3400, hslR, yrfH
Sequence domains: S4 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 10Å
Relevant EMDB volumes: EMD-1455

Quick links

Citations

8 review citations

The bacterial translation stress response.
Starosta et al. (2014)
7 more

1 mention without citation

Structure of Escherichia coli heat shock protein Hsp15 in complex with the ribosomal 50S subunit bearing peptidyl-tRNA.
Safdari et al. (2022)