9JNK
Bacteriophage T4 topoisomerse II bound with a T-segment DNA
Summary for 9JNK
| Entry DOI | 10.2210/pdb9jnk/pdb |
| EMDB information | 61621 |
| Descriptor | DNA topoisomerase large subunit,DNA topoisomerase small subunit, DNA topoisomerase medium subunit, DNA (25-MER), ... (4 entities in total) |
| Functional Keywords | type iia topoisomerase, t-segment dna, isomerase/dna, isomerase-dna complex |
| Biological source | Escherichia phage T4 (Bacteriophage T4) More |
| Total number of polymer chains | 6 |
| Total formula weight | 274298.43 |
| Authors | Xin, Y.H.,Chen, Y.T. (deposition date: 2024-09-23, release date: 2025-10-01, Last modification date: 2026-04-15) |
| Primary citation | Xin, Y.,Xian, R.,Liu, C.,Zhang, O.,Rao, Z.,Li, X.,Chen, Y. Direct trapping of the transport-segment DNA by the central domain of type IIA topoisomerases. Sci Adv, 11:eadw2839-eadw2839, 2025 Cited by PubMed Abstract: Type IIA topoisomerases modulate DNA topology by coordinating the cleavage of gate-segment DNA and the passage of transport-segment DNA-a mechanism conserved across species and essential for diverse cellular processes. While gate-segment interactions have been extensively studied, direct structural evidence of transport-segment capture has remained elusive, limiting our understanding of the full catalytic cycle. Here, we present a cryo-electron microscopy structure of the T4 bacteriophage topoisomerase II with a transport-segment DNA bound directly to its central domain. The structure reveals conformational rearrangements in the central domain that accommodate the transport-segment DNA, suggesting an alternative sequence of events in which the enzyme sliding along the loosely bound religated gate segment may precede transport-segment passage through the coiled-coil gate. Supported by mutational and biochemical assays, our findings provide previously unidentified mechanistic insights and open potential avenues for the development of next-generation type IIA topoisomerase inhibitors. PubMed: 41406217DOI: 10.1126/sciadv.adw2839 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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