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PDBsum entry 3glg
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Transferase/DNA
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PDB id
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3glg
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Contents |
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333 a.a.
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(+ 0 more)
364 a.a.
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334 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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The mechanism of ATP-Dependent primer-Template recognition by a clamp loader complex.
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Authors
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K.R.Simonetta,
S.L.Kazmirski,
E.R.Goedken,
A.J.Cantor,
B.A.Kelch,
R.Mcnally,
S.N.Seyedin,
D.L.Makino,
M.O'Donnell,
J.Kuriyan.
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Ref.
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Cell, 2009,
137,
659-671.
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PubMed id
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Abstract
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Clamp loaders load sliding clamps onto primer-template DNA. The structure of the
E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent
spiral of ATPase domains that tracks only the template strand, allowing
recognition of both RNA and DNA primers. Unlike hexameric helicases, in which
DNA translocation requires distinct conformations of the ATPase domains, the
clamp loader spiral is symmetric and is set up to trigger release upon DNA
recognition. Specificity for primed DNA arises from blockage of the end of the
primer and accommodation of the emerging template along a surface groove. A
related structure reveals how the psi protein, essential for coupling the clamp
loader to single-stranded DNA-binding protein (SSB), binds to the clamp loader.
By stabilizing a conformation of the clamp loader that is consistent with the
ATPase spiral observed upon DNA binding, psi binding promotes the clamp-loading
activity of the complex.
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