7QD8

Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in apo state

Summary for 7QD8

• Entry DOI: 10.2210/pdb7qd8/pdb
• EMDB information: 13906 13908 13909 13910
• Descriptor: Transposase for transposon Tn4430 (1 entity in total)
• Functional Keywords: dna transposition, tn3 family, antibiotic resistance, protein metamorphosis, recombination
• Biological source: Bacillus thuringiensis
• Total number of polymer chains: 2
• Total formula weight: 233844.02

Authors

Shkumatov, A.V.,Oger, C.A.,Aryanpour, N.,Hallet, B.F.,Efremov, R.G. (deposition date: 2021-11-26, release date: 2022-10-26, Last modification date: 2024-07-17)

Primary citation

Shkumatov, A.V.,Aryanpour, N.,Oger, C.A.,Goossens, G.,Hallet, B.F.,Efremov, R.G.
Structural insight into Tn3 family transposition mechanism.
Nat Commun, 13:6155-6155, 2022

PubMed Abstract: Transposons are diverse mobile genetic elements that play the critical role as genome architects in all domains of life. Tn3 is a widespread family and among the first identified bacterial transposons famed for their contribution to the dissemination of antibiotic resistance. Transposition within this family is mediated by a large TnpA transposase, which facilitates both transposition and target immunity. Howtever, a structural framework required for understanding the mechanism of TnpA transposition is lacking. Here, we describe the cryo-EM structures of TnpA from Tn4430 in the apo form and paired with transposon ends before and after DNA cleavage and strand transfer. We show that TnpA has an unusual architecture and exhibits a family specific regulatory mechanism involving metamorphic refolding of the RNase H-like catalytic domain. The TnpA structure, constrained by a double dimerization interface, creates a peculiar topology that suggests a specific role for the target DNA in transpososome assembly and activation.

PubMed: 36257990
DOI: 10.1038/s41467-022-33871-z

Experimental method

ELECTRON MICROSCOPY (3.6 Å)