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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'''SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS'''<br />
'''SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS'''<br />
==Overview==
==Overview==
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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 &lt; 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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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 &lt; 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==
==About this Structure==
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1SSO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SSO OCA].
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1SSO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSO OCA].
==Reference==
==Reference==
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[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:38:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:49 2008''

Revision as of 13:04, 21 February 2008


1sso

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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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