› 1wqg

X-ray diffraction
2.15Å resolution

Crystal structure of ribosome recycling factor from Mycobacterium Tuberculosis

Released:
DOI: 10.2210/pdb1wqg/pdb
PDB entry 1wqg coloured by chain, front view.
PDB entry 1wqg coloured by chain, side view.
PDB entry 1wqg coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications.
Saikrishnan K, Kalapala SK, Varshney U, Vijayan M
J Mol Biol 345 29-38 (2005)
PMID: 15567408

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-recycling factor Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.86 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGY1 (Residues: 1-185; Coverage: 100%)
Gene names: MTCY274.13c, Rv2882c, frr
Sequence domains: Ribosome recycling factor
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CD 3 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 55.499Å b: 33.388Å c: 61.368Å
α: 90° β: 112.42° γ: 90°
R-values:
R R work R free
0.201 0.197 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanism of recycling of post-termination ribosomal complexes in eubacteria: a new role of initiation factor 3.
Seshadri et al. (2006)
17 other articles

1 mention without citation

Ribosome recycling defects modify the balance between the synthesis and assembly of specific subunits of the oxidative phosphorylation complexes in yeast mitochondria.
Ostojić et al. (2016)