2zbk
From Proteopedia
Crystal structure of an intact type II DNA topoisomerase: insights into DNA transfer mechanisms
Overview
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.
About this Structure
2ZBK is a Protein complex structure of sequences from Sulfolobus shibatae. Full crystallographic information is available from OCA.
Reference
Crystal Structure of an Intact Type II DNA Topoisomerase: Insights into DNA Transfer Mechanisms., Graille M, Cladiere L, Durand D, Lecointe F, Gadelle D, Quevillon-Cheruel S, Vachette P, Forterre P, van Tilbeurgh H, Structure. 2008 Mar;16(3):360-70. PMID:18334211 Page seeded by OCA on Wed Apr 9 14:43:57 2008
Categories: Protein complex | Sulfolobus shibatae | Cladiere, L. | Durand, D. | Forterre, P. | Graille, M. | Lecointe, F. | Tilbeurgh, H van. | YSG, Paris-Sud Yeast Structural Genomics. | Atp-binding | Atpase | Decatenation | Dna binding protein | Dna topoisomerase | Dna-binding | Drug design | Magnesium | Metal-binding | Nucleotide-binding | Paris-sud yeast structural genomic | Structural genomic | Ysg