› 2eyq

X-ray diffraction
3.2Å resolution

Crystal structure of Escherichia coli transcription-repair coupling factor

Released:
DOI: 10.2210/pdb2eyq/pdb
PDB entry 2eyq coloured by chain, front view.
PDB entry 2eyq coloured by chain, side view.
PDB entry 2eyq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for bacterial transcription-coupled DNA repair.
Deaconescu AM, Chambers AL, Smith AJ, Nickels BE, Hochschild A, Savery NJ, Darst SA
Cell 124 507-20 (2006)
PMID: 16469698

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription-repair-coupling factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 1151 amino acids
Theoretical weight: 130.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30958 (Residues: 1-1148; Coverage: 100%)
Gene names: JW1100, b1114, mfd
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand EPE 5 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 151.87Å b: 161.99Å c: 161.73Å
α: 90° β: 105.09° γ: 90°
R-values:
R R work R free
0.234 0.234 0.295
Expression system: Escherichia coli

Quick links

Citations

32 review citations

Structure and mechanism of helicases and nucleic acid translocases.
Singleton et al. (2007)
31 more

27 mentions without citation

Prokaryotic nucleotide excision repair.
Kisker et al. (2013)
26 more