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

研究成果: 雜誌貢獻文章同行評審

134 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)782-786
頁數5
期刊Nature Structural Biology
5
發行號9
DOIs
出版狀態已發佈 - 1998
對外發佈

ASJC Scopus subject areas

  • 結構生物學
  • 生物化學
  • 遺傳學

指紋

深入研究「The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA」主題。共同形成了獨特的指紋。

引用此