2ZBK: Crystal Structure Of An Intact Type Ii Dna Topoisomerase: Insights Into Dna Transfer Mechanisms

DNA topoisomerases resolve DNA topological problems created during transcription, replication, and recombination. These ubiquitous enzymes are essential for cell viability and are highly potent targets for the development of antibacterial and antitumoral drugs. Type II enzymes catalyze the transfer of a DNA duplex through another one in an ATP-dependent mechanism. Because of its small size and sensitivity to antitumoral drugs, the archaeal DNA topoisomerase VI, a type II enzyme, is an excellent model for gaining further understanding of the organization and mechanism of these enzymes. We present the crystal structure of intact DNA topoisomerase VI bound to radicicol, an inhibitor of human topo II, and compare it to the conformation of the apo-protein as determined by small-angle X-ray scattering in solution. This structure, combined with a wealth of experimental data gathered on these enzymes, allows us to propose a structural model for the two-gate DNA transfer mechanism.
PDB ID: 2ZBKDownload
MMDB ID: 62398
PDB Deposition Date: 2007/10/22
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 3.56  Å
Source Organism:
Similar Structures:
Biological Unit for 2ZBK: tetrameric; determined by author and by software (PISA)
Molecular Components in 2ZBK
Label Count Molecule
Proteins (4 molecules)
Type II DNA Topoisomerase VI Subunit a
Molecule annotation
Type 2 DNA Topoisomerase 6 Subunit B
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB