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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1995-9-14
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pubmed:abstractText |
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 beta-sheet onto which an orthogonal double-stranded beta-sheet is packed. This topology is very similar to that found in eukaryotic Src homology-3 (SH3) domains. Sso7d binds strongly (Kd < 10 microM) to double-stranded DNA and protects it from thermal denaturation. In addition, we note that epsilon-mono-methylation of lysine side chains of Sso7d is governed by cell growth temperatures, suggesting that methylation is related to the heat-shock response.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
808-19
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7634092-Amino Acid Sequence,
pubmed-meshheading:7634092-Archaeal Proteins,
pubmed-meshheading:7634092-Bacterial Proteins,
pubmed-meshheading:7634092-DNA,
pubmed-meshheading:7634092-DNA-Binding Proteins,
pubmed-meshheading:7634092-Hot Temperature,
pubmed-meshheading:7634092-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7634092-Molecular Sequence Data,
pubmed-meshheading:7634092-Nucleic Acid Denaturation,
pubmed-meshheading:7634092-Protein Binding,
pubmed-meshheading:7634092-Protein Conformation,
pubmed-meshheading:7634092-Sequence Homology, Amino Acid,
pubmed-meshheading:7634092-Solutions,
pubmed-meshheading:7634092-Sulfolobus
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pubmed:year |
1994
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pubmed:articleTitle |
Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus.
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pubmed:affiliation |
Center for Structural Biochemistry, Karolinska Institutet, NOVUM, Huddinge, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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