5BQ5

Crystal structure of the IstB AAA+ domain bound to ADP-BeF3

5BQ5 の概要

• エントリーDOI: 10.2210/pdb5bq5/pdb
• 分子名称: Insertion sequence IS5376 putative ATP-binding protein, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: aaa+, atpase, transposition, dna binding, atp-binding protein
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67462.41

構造登録者

Arias-Palomo, E.,Berger, J.M. (登録日: 2015-05-28, 公開日: 2015-09-02, 最終更新日: 2024-11-06)

主引用文献

Arias-Palomo, E.,Berger, J.M.
An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment.
Cell, 162:860-871, 2015

PubMed Abstract: Transposons are ubiquitous genetic elements that drive genome rearrangements, evolution, and the spread of infectious disease and drug-resistance. Many transposons, such as Mu, Tn7, and IS21, require regulatory AAA+ ATPases for function. We use X-ray crystallography and cryo-electron microscopy to show that the ATPase subunit of IS21, IstB, assembles into a clamshell-shaped decamer that sandwiches DNA between two helical pentamers of ATP-associated AAA+ domains, sharply bending the duplex into a 180° U-turn. Biochemical studies corroborate key features of the structure and further show that the IS21 transposase, IstA, recognizes the IstB•DNA complex and promotes its disassembly by stimulating ATP hydrolysis. Collectively, these studies reveal a distinct manner of higher-order assembly and client engagement by a AAA+ ATPase and suggest a mechanistic model where IstB binding and subsequent DNA bending primes a selected insertion site for efficient transposition.

PubMed: 26276634
DOI: 10.1016/j.cell.2015.07.037

実験手法

X-RAY DIFFRACTION (2.1 Å)