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PDBsum entry 2zub
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Recombination
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PDB id
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2zub
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References listed in PDB file
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Key reference
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Title
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Three new structures of left-Handed rada helical filaments: structural flexibility of n-Terminal domain is critical for recombinase activity.
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Authors
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Y.W.Chang,
T.P.Ko,
C.D.Lee,
Y.C.Chang,
K.A.Lin,
C.S.Chang,
A.H.Wang,
T.F.Wang.
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Ref.
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Plos One, 2009,
4,
e4890.
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PubMed id
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Abstract
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RecA family proteins, including bacterial RecA, archaeal RadA, and eukaryotic
Dmc1 and Rad51, mediate homologous recombination, a reaction essential for
maintaining genome integrity. In the presence of ATP, these proteins bind a
single-strand DNA to form a right-handed nucleoprotein filament, which catalyzes
pairing and strand exchange with a homologous double-stranded DNA (dsDNA), by
as-yet unknown mechanisms. We recently reported a structure of RadA left-handed
helical filament, and here present three new structures of RadA left-handed
helical filaments. Comparative structural analysis between different RadA/Rad51
helical filaments reveals that the N-terminal domain (NTD) of RadA/Rad51,
implicated in dsDNA binding, is highly flexible. We identify a hinge region
between NTD and polymerization motif as responsible for rigid body movement of
NTD. Mutant analysis further confirms that structural flexibility of NTD is
essential for RadA's recombinase activity. These results support our previous
hypothesis that ATP-dependent axial rotation of RadA nucleoprotein helical
filament promotes homologous recombination.
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