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Crystal structure of family 4 uracil–DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding
Author(s) -
Kawai Akito,
Higuchi Shigesada,
Tsunoda Masaru,
Nakamura Kazuo T.,
Yamagata Yuriko,
Miyamoto Shuichi
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.08.019
Subject(s) - uracil dna glycosylase , dna glycosylase , dna , chemistry , intercalation (chemistry) , uracil , dna repair , biochemistry , stereochemistry , inorganic chemistry
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 ( sto UDG). Compared with other UDGs, sto UDG has a different structure of the leucine‐intercalation loop, which is important for DNA binding. The sto UDG–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.