4BT0

MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA transposition

4BT0 の概要

• エントリーDOI: 10.2210/pdb4bt0/pdb
• 関連するPDBエントリー: 4BS1 4BT1
• EMDBエントリー: 2398
• 分子名称: TRANSCRIPTIONAL REGULATOR, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: transcription, aaa+ atpase, dna transposition, nucleoprotein filament, symmetry mismatch
• 由来する生物種: ENTEROBACTERIA PHAGE MU; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28814.70

構造登録者

Mizuno, N.,Dramicanin, M.,Mizuuchi, M.,Adam, J.,Wang, Y.,Han, Y.W.,Yang, W.,Steven, A.C.,Mizuuchi, K.,Ramon-Maiques, S. (登録日: 2013-06-12, 公開日: 2013-07-03, 最終更新日: 2024-05-08)

主引用文献

Mizuno, N.,Dramicanin, M.,Mizuuchi, M.,Adam, J.,Wang, Y.,Han, Y.W.,Yang, W.,Steven, A.C.,Mizuuchi, K.,Ramon-Maiques, S.
Mub is an Aaa+ ATPase that Forms Helical Filaments to Control Target Selection for DNA Transposition.
Proc.Natl.Acad.Sci.USA, 110:E2441-, 2013

PubMed Abstract: MuB is an ATP-dependent nonspecific DNA-binding protein that regulates the activity of the MuA transposase and captures target DNA for transposition. Mechanistic understanding of MuB function has previously been hindered by MuB's poor solubility. Here we combine bioinformatic, mutagenic, biochemical, and electron microscopic analyses to unmask the structure and function of MuB. We demonstrate that MuB is an ATPase associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or without DNA. We also identify critical residues for MuB's ATPase, DNA binding, protein polymerization, and MuA interaction activities. Using single-particle electron microscopy, we show that MuB assembles into a helical filament, which binds the DNA in the axial channel. The helical parameters of the MuB filament do not match those of the coated DNA. Despite this protein-DNA symmetry mismatch, MuB does not deform the DNA duplex. These findings, together with the influence of MuB filament size on strand-transfer efficiency, lead to a model in which MuB-imposed symmetry transiently deforms the DNA at the boundary of the MuB filament and results in a bent DNA favored by MuA for transposition.

PubMed: 23776210
DOI: 10.1073/PNAS.1309499110

実験手法

ELECTRON MICROSCOPY (17 Å)