Crystal Structure of DNA Polymerase β with DNA
Containing the Base Lesion Spiroiminodihydantoin in a Templating Position
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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 <i>S</i> 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 <i>syn</i> 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