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PDBsum entry 4bt0
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Transcription
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PDB id
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4bt0
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References listed in PDB file
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Key reference
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Title
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Mub is an aaa+ atpase that forms helical filaments to control target selection for DNA transposition.
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Authors
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N.Mizuno,
M.Dramićanin,
M.Mizuuchi,
J.Adam,
Y.Wang,
Y.W.Han,
W.Yang,
A.C.Steven,
K.Mizuuchi,
S.Ramón-Maiques.
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Ref.
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Proc Natl Acad Sci U S A, 2013,
110,
E2441.
[DOI no: ]
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PubMed id
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Abstract
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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.
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