› 1aj6

X-ray diffraction
2.3Å resolution

NOVOBIOCIN-RESISTANT MUTANT (R136H) OF THE N-TERMINAL 24 KDA FRAGMENT OF DNA GYRASE B COMPLEXED WITH NOVOBIOCIN AT 2.3 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1aj6/pdb
PDB entry 1aj6 coloured by chain, front view.
PDB entry 1aj6 coloured by chain, side view.
PDB entry 1aj6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study.
Holdgate GA, Tunnicliffe A, Ward WH, Weston SA, Rosenbrock G, Barth PT, Taylor IW, Pauptit RA, Timms D
Biochemistry 36 9663-73 (1997)
PMID: 9245398

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA gyrase subunit B Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 24.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AES6 (Residues: 2-220; Coverage: 27%)
Gene names: JW5625, acrB, b3699, cou, gyrB, himB, hisU, nalC, parA, pcbA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand NOV 1 x NOV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 39.5Å b: 47.72Å c: 114.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.195 0.29
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition.
Jelesarov et al. (1999)
13 more

24 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
23 more