› 3p4x

X-ray diffraction
2.41Å resolution

Helicase domain of reverse gyrase from Thermotoga maritima

Released:
DOI: 10.2210/pdb3p4x/pdb
PDB entry 3p4x coloured by chain, front view.
PDB entry 3p4x coloured by chain, side view.
PDB entry 3p4x coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The conformational flexibility of the helicase-like domain from Thermotoga maritima reverse gyrase is restricted by the topoisomerase domain.
del Toro Duany Y, Klostermeier D, Rudolph MG
Biochemistry 50 5816-23 (2011)
PMID: 21627332

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129368 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Reverse gyrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 413 amino acids
Theoretical weight: 48.09 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: O51934 (Residues: 59-541; Coverage: 37%)
Gene names: TM_0173, rgy, topR
Sequence domains: DEAD/DEAH box helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand ADP 1 x ADP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 59.259Å b: 111.231Å c: 129.726Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.186 0.256
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Reverse gyrase--recent advances and current mechanistic understanding of positive DNA supercoiling.
Lulchev et al. (2014)
2 more

2 mentions without citation

The Evolution of Reverse Gyrase Suggests a Nonhyperthermophilic Last Universal Common Ancestor.
Catchpole et al. (2019)
1 more