8SJD
Cryo-EM structure of the Hermes transposase bound to two right-ends of its DNA transposon.
Summary for 8SJD
| Entry DOI | 10.2210/pdb8sjd/pdb |
| EMDB information | 40553 |
| Descriptor | Hermes transposase, DNA (55-MER), DNA (46-MER), ... (4 entities in total) |
| Functional Keywords | transposase, transpososome, bed domain, protein-dna complex, recombination-dna complex, recombination/dna |
| Biological source | Musca domestica (house fly) More |
| Total number of polymer chains | 10 |
| Total formula weight | 347381.13 |
| Authors | Lannes, L.,Dyda, F. (deposition date: 2023-04-17, release date: 2023-08-02, Last modification date: 2024-06-19) |
| Primary citation | Lannes, L.,Furman, C.M.,Hickman, A.B.,Dyda, F. Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding. Nat Commun, 14:4470-4470, 2023 Cited by PubMed Abstract: The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end. PubMed: 37491363DOI: 10.1038/s41467-023-40210-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.1 Å) |
Structure validation
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