8EDG

Cryo-EM structure of the Hermes transposase bound to two left-ends of its DNA transposon

Summary for 8EDG

• Entry DOI: 10.2210/pdb8edg/pdb
• EMDB information: 28034
• Descriptor: DNA (5'-D(*GP*CP*GP*TP*GP*AP*A)-3'), DNA (46-MER), DNA (55-MER), ... (5 entities in total)
• Functional Keywords: transposase, transpososome, bed domain, protein-dna complex, recombination, recombination-dna complex, recombination/dna
• Biological source: Musca domestica (house fly); More
• Total number of polymer chains: 12
• Total formula weight: 488190.78

Authors

Lannes, L.,Dyda, F. (deposition date: 2022-09-04, 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

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: 37491363
DOI: 10.1038/s41467-023-40210-3

Experimental method

ELECTRON MICROSCOPY (4.64 Å)