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PDBsum entry 4zcf
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Hydrolase-DNA complex
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PDB id
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4zcf
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Contents |
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616 a.a.
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612 a.a.
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627 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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Structural basis of asymmetric DNA methylation and ATP-Triggered long-Range diffusion by ecop15i.
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Authors
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Y.K.Gupta,
S.H.Chan,
S.Y.Xu,
A.K.Aggarwal.
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Ref.
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Nat Commun, 2015,
6,
7363.
[DOI no: ]
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PubMed id
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Abstract
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Type III R-M enzymes were identified >40 years ago and yet there is no
structural information on these multisubunit enzymes. Here we report the
structure of a Type III R-M system, consisting of the entire EcoP15I complex
(Mod2Res1) bound to DNA. The structure suggests how ATP hydrolysis is coupled to
long-range diffusion of a helicase on DNA, and how a dimeric methyltransferase
functions to methylate only one of the two DNA strands. We show that the EcoP15I
motor domains are specifically adapted to bind double-stranded DNA and to
facilitate DNA sliding via a novel 'Pin' domain. We also uncover unexpected
'division of labour', where one Mod subunit recognizes DNA, while the other Mod
subunit methylates the target adenine-a mechanism that may extend to adenine N6
RNA methylation in mammalian cells. Together the structure sheds new light on
the mechanisms of both helicases and methyltransferases in DNA and RNA
metabolism.
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