1sso
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(New page: 200px<br /><applet load="1sso" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sso" /> '''SOLUTION STRUCTURE AND DNA-BINDING PROPERTIE...)
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Revision as of 00:30, 21 November 2007
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SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS
Overview
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.
About this Structure
1SSO is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus., Baumann H, Knapp S, Lundback T, Ladenstein R, Hard T, Nat Struct Biol. 1994 Nov;1(11):808-19. PMID:7634092
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