Crystal structure of the breakage–reunion domain of DNA gyrase

  title={Crystal structure of the breakage–reunion domain of DNA gyrase},
  author={Joo H. Morais Cabral and Andrew P. Jackson and Clare V. Smith and Nita Shikotra and Anthony Maxwell and Robert C. Liddington},
DNA gyrase is a type II DNA topoisomerase from bacteria that introduces supercoils into DNA,. It catalyses the breakage of a DNA duplex (the G segment), the passage of another segment (the T segment) through the break, and then the reunification of the break. This activity involves the opening and closing of a series of molecular ‘gates’ which is coupled to ATP hydrolysis. Here we present the crystal structure of the ‘breakage–reunion’ domain of the gyrase at 2.8 Å resolution. Comparison of the… 
CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage
One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate.
Basic residues at the C-gate of DNA gyrase are involved in DNA supercoiling
  • Eric M. Smith, A. Mondragón
  • Biology
    The Journal of biological chemistry
  • 2021
Crystal structure of DNA gyrase B′ domain sheds lights on the mechanism for T-segment navigation
On the basis of structural analysis and mutation experiments, a sluice-like model for T-segment transport is proposed and it is proposed that a highly conserved pentapeptide mediates large-scale intrasubunit conformational change as a hinge point.
DNA Topoisome Trapping a DNA in Motion
A simplified model for the catalytic cycle in which capture of the transported DNA segment causes conformational changes in the ATPase domain that push the DNA gate open, resulting in stretching and cleaving the gate-DNA in two steps is presented.
Solution structures of DNA-bound gyrase
The proposed gyrase model, with the DNA binding along the sides of the molecule and wrapping around the CTDs located near the exit gate of the protein, adds new information on the mechanism of DNA negative supercoiling.
Control of Strand Scission by Type IIA Topoisomerases
This dissertation helps to explain years of biochemical studies, unifies many elements of topo II mechanism and its control by allostery, and has implications for both understanding large ATP-dependent DNA-remodeling molecular machines as a whole, as well as understanding the means by which small molecules target these enzymes for clinical benefit.
Cryo-EM structure of the complete E. coli DNA Gyrase nucleoprotein complex
This study determined the complete molecular structure of the E. coli DNA Gyrase bound to a 180 bp DNA and the antibiotic Gepotidacin using phase-plate single-particle cryo-electron microscopy and unveils with unprecedented details the structural and spatial organization of the functional domains, their connections and the position of the conserved GyrA-box motif.
A model for the mechanism of strand passage by DNA gyrase.
This work proposes a model in which gyrase captures a contiguous DNA segment with high probability, irrespective of the superhelical density of the DNA substrate, setting up an equilibrium of the transported segment across the DNA gate.


Conversion of DNA gyrase into a conventional type II topoisomerase.
  • S. Kampranis, A. Maxwell
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1996
Results suggest that the unique properties of DNA gyrase are attributable to the wrapping of DNA around the C-terminal DNA-binding domains of the A subunits and provide an insight into the mechanism of type II topoisomerases.
DNA gyrase: structure and function.
In this review, the current knowledge concerning DNA gyrase is summarized by addressing a wide range of aspects of the study of this enzyme.
Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees
The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This
Structure and mechanism of DNA topoisomerase II
The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an
DNA transport by a type II topoisomerase: direct evidence for a two-gate mechanism.
Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed the mechanism for ATP-modulated clamping, and found that a DNA-bound enzyme can admit a second DNA through one set of jaws.
Crystal structure of the met represser–operator complex at 2.8 Å resolution reveals DNA recognition by β-strands
The crystal structure of the met represser–operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment, conferring specificity even for inaccessible base pairs.
Neutron and light-scattering studies of DNA gyrase and its complex with DNA.