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PDBsum entry 4tmu
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Hydrolase/DNA
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PDB id
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4tmu
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References listed in PDB file
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Key reference
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Title
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Structural mechanisms of DNA binding and unwinding in bacterial recq helicases.
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Authors
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K.A.Manthei,
M.C.Hill,
J.E.Burke,
S.E.Butcher,
J.L.Keck.
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Ref.
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Proc Natl Acad Sci U S A, 2015,
112,
4292-4297.
[DOI no: ]
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PubMed id
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Abstract
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RecQ helicases unwind remarkably diverse DNA structures as key components of
many cellular processes. How RecQ enzymes accommodate different substrates in a
unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here,
the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core
domain bound to duplex DNA with a 3' single-stranded extension identifies two
DNA-dependent conformational rearrangements: a winged-helix domain pivots
∼90° to close onto duplex DNA, and a conserved aromatic-rich loop is
remodeled to bind ssDNA. These changes coincide with a restructuring of the RecQ
ATPase active site that positions catalytic residues for ATP hydrolysis. Complex
formation also induces a tight bend in the DNA and melts a portion of the
duplex. This bending, coupled with translocation, could provide RecQ with a
mechanism for unwinding duplex and other DNA structures.
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