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PDBsum entry 5tyc
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Transferase/DNA
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PDB id
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5tyc
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References listed in PDB file
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Key reference
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Title
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Time-Lapse crystallography snapshots of a double-Strand break repair polymerase in action.
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Authors
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J.A.Jamsen,
W.A.Beard,
L.C.Pedersen,
D.D.Shock,
A.F.Moon,
J.M.Krahn,
K.Bebenek,
T.A.Kunkel,
S.H.Wilson.
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Ref.
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Nat Commun, 2017,
8,
253.
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PubMed id
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Abstract
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DNA polymerase (pol) μ is a DNA-dependent polymerase that incorporates
nucleotides during gap-filling synthesis in the non-homologous end-joining
pathway of double-strand break repair. Here we report time-lapse X-ray
crystallography snapshots of catalytic events during gap-filling DNA synthesis
by pol μ. Unique catalytic intermediates and active site conformational changes
that underlie catalysis are uncovered, and a transient third (product) metal ion
is observed in the product state. The product manganese coordinates phosphate
oxygens of the inserted nucleotide and PPi. The product metal is not
observed during DNA synthesis in the presence of magnesium. Kinetic analyses
indicate that manganese increases the rate constant for deoxynucleoside
5'-triphosphate insertion compared to magnesium. The likely product
stabilization role of the manganese product metal in pol μ is discussed. These
observations provide insight on structural attributes of this X-family
double-strand break repair polymerase that impact its biological function in
genome maintenance.DNA polymerase (pol) μ functions in DNA double-strand break
repair. Here the authors use time-lapse X-ray crystallography to capture the
states of pol µ during the conversion from pre-catalytic to product complex and
observe a third transiently bound metal ion in the product state.
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