8QQU
Asymetric subunit of E. coli DNA gyrase bound to a linear part of a DNA minicircle
Summary for 8QQU
| Entry DOI | 10.2210/pdb8qqu/pdb |
| EMDB information | 18605 |
| Descriptor | DNA gyrase subunit A, DNA gyrase subunit B, DNA (16-MER), ... (4 entities in total) |
| Functional Keywords | dna-protein complex, type iia topoisomerase, dna gyrase, isomerase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 196934.98 |
| Authors | Vayssieres, M.,Lamour, V. (deposition date: 2023-10-06, release date: 2024-04-10, Last modification date: 2024-04-24) |
| Primary citation | Vayssieres, M.,Marechal, N.,Yun, L.,Lopez Duran, B.,Murugasamy, N.K.,Fogg, J.M.,Zechiedrich, L.,Nadal, M.,Lamour, V. Structural basis of DNA crossover capture by Escherichia coli DNA gyrase. Science, 384:227-232, 2024 Cited by PubMed Abstract: DNA supercoiling must be precisely regulated by topoisomerases to prevent DNA entanglement. The interaction of type IIA DNA topoisomerases with two DNA molecules, enabling the transport of one duplex through the transient double-stranded break of the other, remains elusive owing to structures derived solely from single linear duplex DNAs lacking topological constraints. Using cryo-electron microscopy, we solved the structure of DNA gyrase bound to a negatively supercoiled minicircle DNA. We show how DNA gyrase captures a DNA crossover, revealing both conserved molecular grooves that accommodate the DNA helices. Together with molecular tweezer experiments, the structure shows that the DNA crossover is of positive chirality, reconciling the binding step of gyrase-mediated DNA relaxation and supercoiling in a single structure. PubMed: 38603484DOI: 10.1126/science.adl5899 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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