› 4xtj

X-ray diffraction
1.92Å resolution

N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition

Released:
DOI: 10.2210/pdb4xtj/pdb
PDB entry 4xtj coloured by chain, front view.
PDB entry 4xtj coloured by chain, side view.
PDB entry 4xtj coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The role of monovalent cations in the ATPase reaction of DNA gyrase.
Hearnshaw SJ, Chung TT, Stevenson CE, Maxwell A, Lawson DM
Acta Crystallogr D Biol Crystallogr 71 996-1005 (2015)
PMID: 25849408

Function and Biology Details

Reaction catalysed: 
ATP-dependent breakage, passage and rejoining of double-stranded DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA gyrase subunit B Chain: A
Molecule details ›
Chain: A
Length: 391 amino acids
Theoretical weight: 43.16 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AES6 (Residues: 2-392; Coverage: 49%)
Gene names: JW5625, acrB, b3699, cou, gyrB, himB, hisU, nalC, parA, pcbA
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ANP 1 x ANP
Ligand MG 1 x MG
Ligand K 1 x K
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 87.52Å b: 140.91Å c: 79.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 citation in other articles

Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity.
Elnatan et al. (2018)
8 more

3 mentions without citation

The role of monovalent cations in the ATPase reaction of DNA gyrase.
Hearnshaw et al. (2015)
2 more