› 1f4k

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX

Released:
DOI: 10.2210/pdb1f4k/pdb
PDB entry 1f4k coloured by chain, front view.
PDB entry 1f4k coloured by chain, side view.
PDB entry 1f4k coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest.
Wilce JA, Vivian JP, Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC
Nat Struct Biol 8 206-10 (2001)
PMID: 11224562

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113787 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Replication termination protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 122 amino acids
Theoretical weight: 14.53 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CI76 (Residues: 1-122; Coverage: 100%)
Gene names: BSU18490, rtp
Sequence domains: Replication terminator protein
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
5'-D(*CP*TP*AP*TP*GP*AP*AP*CP*AP*TP*AP*AP*TP*GP*TP*TP*CP*AP*TP*AP*G)-3' Chain: D
Molecule details ›
Chain: D
Length: 21 nucleotides
Theoretical weight: 6.45 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
5'-D(*CP*TP*AP*TP*GP*AP*AP*CP*AP*TP*TP*AP*TP*GP*TP*TP*CP*AP*TP*AP*G)-3' Chain: E
Molecule details ›
Chain: E
Length: 21 nucleotides
Theoretical weight: 6.44 KDa
Source organism: Bacillus subtilis
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P3221
Unit cell:
a: 44.78Å b: 44.78Å c: 395.58Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.271 0.228 0.276
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

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

14 mentions without citation

Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.
Robinson et al. (2012)
13 more