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

Abstract

Sso7d and Sac7d are two small (~7,000 Mr), 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 Tm of DNA by ~40 °C. Sso7d in complex with GTAATTAC and GCGT(iU)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.

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Figure 1: a, Amino acid sequences of recombinant Sso7d and Sac7d.
Figure 2: a, Stereoscopic surface drawing of the electrostatic potential of the Sso7d–GCGT(iU)CGC + GCGAACGC complex.
Figure 3: a, Detailed local structures at the protein–DNA interface of the Sso7d– GCGT(iU)CGC + GCGAACGC complex.
Figure 4: Stereoscopic view of the intercalation sites.

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Acknowledgements

This work was supported by the NIH (A.H.J.W. and J.W.S.).

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Correspondence to Andrew H.-J. Wang.

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Gao, YG., Su, SY., Robinson, H. et al. The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA. Nat Struct Mol Biol 5, 782–786 (1998). https://doi.org/10.1038/1822

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