› 1t3w

X-ray diffraction
2.8Å resolution

Crystal Structure of the E.coli DnaG C-terminal domain (residues 434 to 581)

Released:
DOI: 10.2210/pdb1t3w/pdb
PDB entry 1t3w coloured by chain, front view.
PDB entry 1t3w coloured by chain, side view.
PDB entry 1t3w coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal and solution structures of the helicase-binding domain of Escherichia coli primase.
Oakley AJ, Loscha KV, Schaeffer PM, Liepinsh E, Pintacuda G, Wilce MC, Otting G, Dixon NE
J Biol Chem 280 11495-504 (2005)
PMID: 15649896

Function and Biology Details

Reaction catalysed: 
SsDNA + n NTP = ssDNA/pppN(pN)(n-1) hybrid + (n-1) diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-142202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA primase Chains: A, B
Molecule details ›
Chains: A, B
Length: 148 amino acids
Theoretical weight: 16.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABS5 (Residues: 434-581; Coverage: 26%)
Gene names: JW3038, b3066, dnaG, dnaP, parB
Sequence domains: DNA primase DnaG DnaB-binding
Structure domains: DNAb Helicase; Chain A

Ligands and Environments

1 bound ligand:
Ligand ACY 1 x ACY
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: I4122
Unit cell:
a: 142.239Å b: 142.239Å c: 192.131Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.271 0.269 0.308
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

SSB as an organizer/mobilizer of genome maintenance complexes.
Shereda et al. (2008)
12 more

9 mentions without citation

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