› 1osb

X-ray diffraction
2.65Å resolution

Conjugative Relaxase TrwC in complex with OriT Dna. Metal-free structure.

Released:
DOI: 10.2210/pdb1osb/pdb
PDB entry 1osb coloured by chain, front view.
PDB entry 1osb coloured by chain, side view.
PDB entry 1osb coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.
Guasch A, Lucas M, Moncalián G, Cabezas M, Pérez-Luque R, Gomis-Rüth FX, de la Cruz F, Coll M
Nat Struct Biol 10 1002-10 (2003)
PMID: 14625590

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114322 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
TrwC relaxase domain-containing protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 293 amino acids
Theoretical weight: 32.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47673 (Residues: 1-293; Coverage: 30%)
Gene name: trwC
Sequence domains: TrwC relaxase
Dna oligonucleotide Chains: B, D
Molecule details ›
Chains: B, D
Length: 25 nucleotides
Theoretical weight: 7.71 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 9 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P65
Unit cell:
a: 147.78Å b: 147.78Å c: 78.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.195 0.241
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

21 review citations

Mobility of plasmids.
Smillie et al. (2010)
20 more

3 mentions without citation

Identification of a Kupffer cell subset capable of reverting the T cell dysfunction induced by hepatocellular priming.
De Simone et al. (2021)
2 more