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9O8Z

CryoEM structure of M. mazei topoisomerase VI-minicircle DNA complex in partially unfolded transducer state

Summary for 9O8Z
Entry DOI10.2210/pdb9o8z/pdb
EMDB information70239
DescriptorType 2 DNA topoisomerase 6 subunit A, Type 2 DNA topoisomerase 6 subunit B, Minicircle DNA (arbitrary model sequence), ... (6 entities in total)
Functional Keywordstoprim, ghkl, minicircle dna, spo11, isomerase-dna complex, isomerase/dna
Biological sourceMethanosarcina mazei Go1
More
Total number of polymer chains6
Total formula weight268826.47
Authors
Richman, D.E.,Berger, J.M. (deposition date: 2025-04-17, release date: 2026-02-25, Last modification date: 2026-04-08)
Primary citationRichman, D.E.,Wendorff, T.J.,Rashid, F.,Beck, C.,Yan, Q.,Johnson, H.R.,Eckerty, R.A.,Fogg, J.M.,Baker, M.L.,Zechiedrich, L.,Berger, J.M.
Supercoiled DNA recognition and cleavage control in topoisomerase VI.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: Type II topoisomerases modulate DNA supercoiling and resolve chromosome entanglements. Type IIB topoisomerases, exemplified by DNA topoisomerase VI (Top6), are used by plants and archaea to support endoreduplication and cell proliferation, respectively; homologs of Top6 further serve to initiate meiotic recombination in eukaryotes and constitute the nuclease portion of MksBEFG/Wadjet/Gabija bacterial defense systems. To understand how such factors act upon DNA, we determine structures of Top6 bound to supercoiled minicircles in cleaved and uncleaved states using single-particle electron cryo-microscopy. The structures show that Top6 binds a curved 74 bp region of the supercoiled minicircle DNA and that it cuts at a distinct deformability motif, explaining its preference for supercoiled substrates and highlighting the role of DNA plasticity in cleavage site selection. Dynamic protein-DNA interactions and an unanticipated tension sensor help recognize bent DNA and couple ATPase disposition to cleavage state activation. Our observations explain how DNA recognition and cleavage by type II topoisomerases are regulated by interdependent structural changes in DNA and the enzyme.
PubMed: 41698922
DOI: 10.1038/s41467-026-69491-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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