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PDBsum entry 6raw
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Contents |
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603 a.a.
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585 a.a.
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608 a.a.
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576 a.a.
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601 a.a.
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631 a.a.
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542 a.a.
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195 a.a.
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171 a.a.
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162 a.a.
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203 a.a.
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References listed in PDB file
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Key reference
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Title
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Molecular basis for ATP-Hydrolysis-Driven DNA translocation by the cmg helicase of the eukaryotic replisome.
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Authors
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P.Eickhoff,
H.B.Kose,
F.Martino,
T.Petojevic,
F.Abid ali,
J.Locke,
N.Tamberg,
A.Nans,
J.M.Berger,
M.R.Botchan,
H.Yardimci,
A.Costa.
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Ref.
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Cell Rep, 2019,
28,
2673.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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In the eukaryotic replisome, DNA unwinding by the Cdc45-MCM-Go-Ichi-Ni-San
(GINS) (CMG) helicase requires a hexameric ring-shaped ATPase named
minichromosome maintenance (MCM), which spools single-stranded DNA through its
central channel. Not all six ATPase sites are required for unwinding; however,
the helicase mechanism is unknown. We imaged ATP-hydrolysis-driven translocation
of the CMG using cryo-electron microscopy (cryo-EM) and found that the six MCM
subunits engage DNA using four neighboring protomers at a time, with ATP binding
promoting DNA engagement. Morphing between different helicase states leads us to
suggest a non-symmetric hand-over-hand rotary mechanism, explaining the
asymmetric requirements of ATPase function around the MCM ring of the CMG. By
imaging of a higher-order replisome assembly, we find that the Mrc1-Csm3-Tof1
fork-stabilization complex strengthens the interaction between parental duplex
DNA and the CMG at the fork, which might support the coupling between DNA
translocation and fork unwinding.
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