Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.

@article{Yamasaki2010SolutionSO,
  title={Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.},
  author={Kazuhiko Yamasaki and Yuji Urushibata and Tomoko Yamasaki and Fumio Arisaka and Ikuo Matsui},
  journal={FEBS letters},
  year={2010},
  volume={584 15},
  pages={3370-5}
}
Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. We analyzed the structure of the N-terminal 200 amino-acid regulatory region of the small subunit by NMR and revealed that the N-terminal approximately 70 amino-acid region is folded. The structure consists of a four-alpha-helix bundle including a short parallel beta-sheet, which is similar to the N-terminal regions of the B subunits of human DNA… CONTINUE READING

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