Crystal structure of family 4 uracil-DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding

Akito Kawai, Shigesada Higuchi, Masaru Tsunoda, Kazuo T. Nakamura, Yuriko Yamagata, Shuichi Miyamoto

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2675-2682
Number of pages8
JournalFEBS Letters
Volume589
Issue number19
DOIs
Publication statusPublished - 14-09-2015
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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