Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs

Shaoyu Su, Yi Gui Gao, Howard Robinson, Yen Chywan Liaw, Stephen P. Edmondson, John W. Shriver, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 Å, 2.2 Å and 2.2 Å, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)395-403
Number of pages9
JournalJournal of Molecular Biology
Volume303
Issue number3
DOIs
Publication statusPublished - Oct 27 2000
Externally publishedYes

Keywords

  • Achaeabacteria
  • DNA binding protein
  • Hyperthermophile
  • Protein stability
  • Protein-DNA interactions

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

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