Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
- 1 November 1994
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 1 (11) , 808-819
- https://doi.org/10.1038/nsb1194-808
Abstract
The archaeon Sulfolobus solfataricus expresses large amounts of a small basic protein, Sso7d, which was previously identified as a DNA-binding protein possibly involved in compaction of DNA. We have determined the solution structure of Sso7d. The protein consists of a triple-stranded anti-parallel β-sheet onto which an orthogonal double-stranded β-sheet is packed. This topology is very similar to that found in eukaryotic Src homology-3 (SH3) domains. Sso7d binds strongly (Kd < 10 μM) to double-stranded DNA and protects it from thermal denaturation. In addition, we note that ɛ-mono-methylation of lysine side chains of Sso7d is governed by cell growth temperatures, suggesting that methylation is related to the heat-shock response.Keywords
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