The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA

Y. G. Gao, S. Y. Su, H. Robinson, S. Padmanabhan, L. Lim, B. S. McCrary, S. P. Edmondson, J. W. Shriver, A. H.J. Wang

Research output: Contribution to journalArticlepeer-review

134 Citations (Scopus)

Abstract

Sso7d and Sac7d are two small (~7,000 M(r)), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the T(m) of DNA by ~40 °C. Sso7d in complex with GTAATTAC and GCGT((i)U)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (~60°) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing.

Original languageEnglish
Pages (from-to)782-786
Number of pages5
JournalNature Structural Biology
Volume5
Issue number9
DOIs
Publication statusPublished - 1998
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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