Crystal structure of DNA polymerase β with DNA containing the base lesion spiroiminodihydantoin in a templating position

Brian E. Eckenroth, Aaron M. Fleming, Joann B. Sweasy, Cynthia J. Burrows, Sylvie Doublié

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

The first high-resolution crystal structure of spiroiminodihydantoin (dSp1) was obtained in the context of the DNA polymerase β active site and reveals two areas of significance. First, the structure verifies the recently determined S configuration at the spirocyclic carbon. Second, the distortion of the DNA duplex is similar to that of the single-oxidation product 8-oxoguanine. For both oxidized lesions, adaptation of the syn conformation results in similar backbone distortions in the DNA duplex. The resulting conformation positions the dSp1 A-ring as the base-pairing face whereas the B-ring of dSp1 protrudes into the major groove.

Original languageEnglish (US)
Pages (from-to)2075-2077
Number of pages3
JournalBiochemistry
Volume53
Issue number13
DOIs
StatePublished - Apr 8 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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