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 language | English |
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Pages (from-to) | 395-403 |
Number of pages | 9 |
Journal | Journal of Molecular Biology |
Volume | 303 |
Issue number | 3 |
DOIs | |
Publication status | Published - Oct 27 2000 |
Externally published | Yes |
Keywords
- Achaeabacteria
- DNA binding protein
- Hyperthermophile
- Protein stability
- Protein-DNA interactions
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology