› 2aar

X-ray diffraction
3.5Å resolution

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome.

Released:
DOI: 10.2210/pdb2aar/pdb
PDB entry 2aar coloured by chain, front view.
PDB entry 2aar coloured by chain, side view.
PDB entry 2aar coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action.
Baram D, Pyetan E, Sittner A, Auerbach-Nevo T, Bashan A, Yonath A
Proc Natl Acad Sci U S A 102 12017-22 (2005)
PMID: 16091460

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-193261 (preferred)
Entry contents:
3 distinct polypeptide molecules
1 distinct RNA molecule
Macromolecules (4 distinct):
Large ribosomal subunit protein uL23 Chain: R
Molecule details ›
Chain: R
Length: 95 amino acids
Theoretical weight: 10.54 KDa
Source organism: Deinococcus radiodurans
UniProt:
  • Canonical: Q9RXK0 (Residues: 1-95; Coverage: 100%)
Gene names: DR_0313, rplW
Sequence domains: Ribosomal protein L23
Large ribosomal subunit protein uL29 Chain: W
Molecule details ›
Chain: W
Length: 67 amino acids
Theoretical weight: 7.77 KDa
Source organism: Deinococcus radiodurans
UniProt:
  • Canonical: Q9RXJ4 (Residues: 1-67; Coverage: 100%)
Gene names: DR_0319, rpmC
Sequence domains: Ribosomal L29 protein
Trigger factor Chain: 7
Molecule details ›
Chain: 7
Length: 113 amino acids
Theoretical weight: 12.59 KDa
Source organism: Deinococcus radiodurans
UniProt:
  • Canonical: Q9RT21 (Residues: 2-114; Coverage: 24%)
Gene names: DR_1948, tig
Sequence domains: Bacterial trigger factor protein (TF)
23S ribosomal RNA Chain: 0
Molecule details ›
Chain: 0
Length: 2880 nucleotides
Theoretical weight: 933.41 KDa
Sequence domains: Bacterial large subunit ribosomal RNA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 169.386Å b: 407.063Å c: 692.746Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.251 0.32

Quick links

Citations

18 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
17 more

11 mentions without citation

Differential targeting and retention of G protein-coupled receptors in polarized epithelial cells.
Wozniak et al. (1997)
10 more