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PDBsum entry 4zby
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References listed in PDB file
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Key reference
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Title
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Crystal structure of family 4 uracil-Dna glycosylase from sulfolobus tokodaii and a function of tyrosine 170 in DNA binding.
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Authors
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A.Kawai,
S.Higuchi,
M.Tsunoda,
K.T.Nakamura,
Y.Yamagata,
S.Miyamoto.
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Ref.
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Febs Lett, 2015,
589,
2675-2682.
[DOI no: ]
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PubMed id
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Abstract
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Uracil-DNA glycosylases (UDGs) excise uracil from DNA by catalyzing the
N-glycosidic bond hydrolysis. Here we report the first crystal structures of an
archaeal UDG (stoUDG). Compared with other UDGs, stoUDG has a different
structure of the leucine-intercalation loop, which is important for DNA binding.
The stoUDG-DNA complex model indicated that Leu169, Tyr170, and Asn171 in the
loop are involved in DNA intercalation. Mutational analysis showed that Tyr170
is critical for substrate DNA recognition. These results indicate that Tyr170
occupies the intercalation site formed after the structural change of the
leucine-intercalation loop required for the catalysis.
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