› 1nlf

X-ray diffraction
1.95Å resolution

Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution

Released:
DOI: 10.2210/pdb1nlf/pdb
PDB entry 1nlf coloured by chain, front view.
PDB entry 1nlf coloured by chain, side view.
PDB entry 1nlf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of DNA helicase RepA in complex with sulfate at 1.95 A resolution implicates structural changes to an "open" form.
Xu H, Sträter N, Schröder W, Böttcher C, Ludwig K, Saenger W
Acta Crystallogr D Biol Crystallogr 59 815-22 (2003)
PMID: 12777796

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148960 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulatory protein RepA Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 279 amino acids
Theoretical weight: 29.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P20356 (Residues: 1-279; Coverage: 100%)
Gene name: repA
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2
Unit cell:
a: 192.3Å b: 55.3Å c: 105.6Å
α: 90° β: 122.9° γ: 90°
R-values:
R R work R free
0.236 0.201 0.242
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex.
Neylon et al. (2005)
1 more

2 mentions without citation

Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.
Chatterjee et al. (2009)
1 more