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PDBsum entry 2boo
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References listed in PDB file
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Key reference
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Title
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Structure of the uracil-Dna n-Glycosylase (ung) from deinococcus radiodurans.
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Authors
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I.Leiros,
E.Moe,
A.O.Smalås,
S.Mcsweeney.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2005,
61,
1049-1056.
[DOI no: ]
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PubMed id
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Abstract
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Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of
promutagenic uracil from single- and double-stranded DNA, thereby initiating the
base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation
of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine,
resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus
radiodurans has an elevated number of uracil-DNA glycosylases compared with most
other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase),
which has been shown to be the major contributor to the removal of
mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is
reported.
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Figure 2.
Figure 2
Ribbon illustration of the crystal structure of drUNG. The nitrate molecules are shown as
ball-and-stick representations in atom colour, with the one bound in the active site
labelled in bold.
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Figure 5.
Figure 5
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
1049-1056)
copyright 2005.
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