7MBW

Crystal structure of TnsC(1-503)A225V

7MBW の概要

• エントリーDOI: 10.2210/pdb7mbw/pdb
• 分子名称: Transposon Tn7 transposition protein TnsC, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: aaa+ atpase, transposition, dna binding, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 241444.92

構造登録者

Shen, Y.,Guarne, A. (登録日: 2021-04-01, 公開日: 2022-02-23, 最終更新日: 2024-11-06)

主引用文献

Shen, Y.,Gomez-Blanco, J.,Petassi, M.T.,Peters, J.E.,Ortega, J.,Guarne, A.
Structural basis for DNA targeting by the Tn7 transposon.
Nat.Struct.Mol.Biol., 29:143-151, 2022

PubMed Abstract: Tn7 transposable elements are unique for their highly specific, and sometimes programmable, target-site selection mechanisms and precise insertions. All the elements in the Tn7 family utilize an AAA+ adaptor (TnsC) to coordinate target-site selection with transpososome assembly and to prevent insertions at sites already containing a Tn7 element. Owing to its multiple functions, TnsC is considered the linchpin in the Tn7 element. Here we present the high-resolution cryo-EM structure of TnsC bound to DNA using a gain-of-function variant of the protein and a DNA substrate that together recapitulate the recruitment to a specific DNA target site. TnsC forms an asymmetric ring on target DNA that segregates target-site selection and interaction with the paired-end complex to opposite faces of the ring. Unlike most AAA+ ATPases, TnsC uses a DNA distortion to find the target site but does not remodel DNA to activate transposition. By recognizing pre-distorted substrates, TnsC creates a built-in regulatory mechanism where ATP hydrolysis abolishes ring formation proximal to an existing element. This work unveils how Tn7 and Tn7-like elements determine the strict spacing between the target and integration sites.

PubMed: 35173349
DOI: 10.1038/s41594-022-00724-8

実験手法

X-RAY DIFFRACTION (3.2 Å)