7QD5

Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with 48 bp long transposon end DNA

7QD5 の概要

• エントリーDOI: 10.2210/pdb7qd5/pdb
• EMDBエントリー: 13906 13908
• 分子名称: Transposase for transposon Tn4430, IR48 DNA substrate, non transferred strand, IR48 transferred strand (3 entities in total)
• 機能のキーワード: dna transposition, tn3 family, antibiotic resistance, protein metamorphosis, recombination
• 由来する生物種: Bacillus thuringiensis; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 293124.15

構造登録者

Shkumatov, A.V.,Oger, C.A.,Aryanpour, N.,Hallet, B.F.,Efremov, R.G. (登録日: 2021-11-26, 公開日: 2022-10-26, 最終更新日: 2024-07-17)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.1 Å)