› 4wuc

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb4wuc/pdb
PDB 4wuc coloured by chain and viewed from the front.
PDB 4wuc coloured by chain and viewed from the side.
PDB 4wuc coloured by chain and viewed from the top.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA gyrase subunit B Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 43.32 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AES6 (Residues: 2-393; Coverage: 49%)
Gene names: JW5625, acrB, b3699, cou, gyrB, himB, hisU, nalC, parA, pcbA
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ANP 1 x ANP
Ligand MG 1 x MG
Ligand NA 2 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2221
Unit cell:
a: 87.91Å b: 140.88Å c: 79.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.22
Expression system: Escherichia coli BL21(DE3)

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Citations

8 citation in other articles

A comprehensive structural analysis of the ATPase domain of human DNA topoisomerase II beta bound to AMPPNP, ADP, and the bisdioxopiperazine, ICRF193.
Ling et al. (2022)
7 more

2 mentions without citation

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