1D3Y

STRUCTURE OF THE DNA TOPOISOMERASE VI A SUBUNIT

Summary for 1D3Y

• Entry DOI: 10.2210/pdb1d3y/pdb
• Descriptor: DNA TOPOISOMERASE VI A SUBUNIT, SODIUM ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: topoisomerase vi, dna binding protein, spo11 homolog, isomerase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 2
• Total formula weight: 68316.46

Authors

Nichols, M.D.,DeAngelis, K.A.,Keck, J.L.,Berger, J.M. (deposition date: 1999-10-01, release date: 1999-11-05, Last modification date: 2024-02-07)

Primary citation

Nichols, M.D.,DeAngelis, K.,Keck, J.L.,Berger, J.M.
Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11.
EMBO J., 18:6177-6188, 1999

PubMed Abstract: In all organisms, type II DNA topoisomerases are essential for untangling chromosomal DNA. We have determined the structure of the DNA-binding core of the Methanococcus jannaschii DNA topoisomerase VI A subunit at 2.0 A resolution. The overall structure of this subunit is unique, demonstrating that archaeal type II enzymes are distinct from other type II topoisomerases. However, the core structure contains a pair of domains that are also found in type IA and classic type II topoisomerases. Together, these regions may form the basis of a DNA cleavage mechanism shared among these enzymes. The core A subunit is a dimer that contains a deep groove that spans both protomers. The dimer architecture suggests that DNA is bound in the groove, across the A subunit interface, and that the two monomers separate during DNA transport. The A subunit of topoisomerase VI is homologous to the meiotic recombination factor, Spo11, and this structure can serve as a template for probing Spo11 function in eukaryotes.

PubMed: 10545127
DOI: 10.1093/emboj/18.21.6177

Experimental method

X-RAY DIFFRACTION (2 Å)