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

doi:10.1038/1822

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 journal › Article › peer-review

138 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 language	English
Pages (from-to)	782-786
Number of pages	5
Journal	Nature Structural Biology
Volume	5
Issue number	9
DOIs	https://doi.org/10.1038/1822
Publication status	Published - 1998
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA",

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.",

author = "Gao, {Y. G.} and Su, {S. Y.} and H. Robinson and S. Padmanabhan and L. Lim and McCrary, {B. S.} and Edmondson, {S. P.} and Shriver, {J. W.} and Wang, {A. H.J.}",

note = "Funding Information: This work was supported by the NIH (A.H.J.W. and J.W.S.).",

year = "1998",

doi = "10.1038/1822",

language = "English",

volume = "5",

pages = "782--786",

journal = "Nature Structural Biology",

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T1 - The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA

AU - Gao, Y. G.

AU - Su, S. Y.

AU - Robinson, H.

AU - Padmanabhan, S.

AU - Lim, L.

AU - McCrary, B. S.

AU - Edmondson, S. P.

AU - Shriver, J. W.

AU - Wang, A. H.J.

N1 - Funding Information: This work was supported by the NIH (A.H.J.W. and J.W.S.).

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

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JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 9

ER -

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

Abstract

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