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PDBsum entry 1yjm
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Transferase/DNA binding protein
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PDB id
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1yjm
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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 molecular architecture of the mammalian DNA repair enzyme, Polynucleotide kinase.
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Authors
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N.K.Bernstein,
R.S.Williams,
M.L.Rakovszky,
D.Cui,
R.Green,
F.Karimi-Busheri,
R.S.Mani,
S.Galicia,
C.A.Koch,
C.E.Cass,
D.Durocher,
M.Weinfeld,
J.N.Glover.
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Ref.
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Mol Cell, 2005,
17,
657-670.
[DOI no: ]
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PubMed id
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Abstract
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Mammalian polynucleotide kinase (PNK) is a key component of both the base
excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways.
PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl
termini, which are a necessary prerequisite for ligation during repair. PNK is
recruited to repair complexes through interactions between its N-terminal FHA
domain and phosphorylated components of either pathway. Here, we describe the
crystal structure of intact mammalian PNK and a structure of the PNK FHA bound
to a cognate phosphopeptide. The kinase domain has a broad substrate binding
pocket, which preferentially recognizes double-stranded substrates with recessed
5' termini. In contrast, the phosphatase domain efficiently dephosphorylates
single-stranded 3'-phospho termini as well as double-stranded substrates. The
FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible
tether, and it exhibits a mode of target selection based on electrostatic
complementarity between the binding surface and the phosphothreonine peptide.
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Figure 1.
Figure 1. Structure of Mouse PNK
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Figure 3.
Figure 3. The Kinase Domain
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
17,
657-670)
copyright 2005.
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