- EMDB-38696: CryoEM structure of ADP-DNA-MuB conformation1 -
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基本情報
登録情報
データベース: EMDB / ID: EMD-38696
タイトル
CryoEM structure of ADP-DNA-MuB conformation1
マップデータ
CryoEM structure of ADP-DNA-MuB conformation1 with D9
試料
複合体: ADP-DNA-MuB conformation1
タンパク質・ペプチド: ATP-dependent target DNA activator B
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
MuB / MuB-ADP / Ring / VIRAL PROTEIN
機能・相同性
機能・相同性情報
DNA transposition / viral DNA genome replication / 加水分解酵素; 酸無水物に作用; リン含有酸無水物に作用 / DNA integration / host cell cytoplasm / DNA replication / ATP hydrolysis activity / DNA binding / ATP binding / metal ion binding 類似検索 - 分子機能
B transposition protein, C-terminal / B transposition protein, C-terminal domain superfamily / Mu B transposition protein, C terminal / : / : / AAA domain / Lambda repressor-like, DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
ジャーナル: Nat Commun / 年: 2024 タイトル: Elucidating the Architectural dynamics of MuB filaments in bacteriophage Mu DNA transposition. 著者: Xiaolong Zhao / Yongxiang Gao / Qingguo Gong / Kaiming Zhang / Shanshan Li / 要旨: MuB is a non-specific DNA-binding protein and AAA+ ATPase that significantly influences the DNA transposition process of bacteriophage Mu, especially in target DNA selection for transposition. While ...MuB is a non-specific DNA-binding protein and AAA+ ATPase that significantly influences the DNA transposition process of bacteriophage Mu, especially in target DNA selection for transposition. While studies have established the ATP-dependent formation of MuB filament as pivotal to this process, the high-resolution structure of a full-length MuB protomer and the underlying molecular mechanisms governing its oligomerization remain elusive. Here, we use cryo-EM to obtain a 3.4-Å resolution structure of the ATP(+)-DNA(+)-MuB helical filament, which encapsulates the DNA substrate within its axial channel. The structure categorizes MuB within the initiator clade of the AAA+ protein family and precisely locates the ATP and DNA binding sites. Further investigation into the oligomeric states of MuB show the existence of various forms of the filament. These findings lead to a mechanistic model where MuB forms opposite helical filaments along the DNA, exposing potential target sites on the bare DNA and then recruiting MuA, which stimulates MuB's ATPase activity and disrupts the previously formed helical structure. When this happens, MuB generates larger ring structures and dissociates from the DNA.