2ihf

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(New page: 200px<br /><applet load="2ihf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihf, resolution 1.90&Aring;" /> '''Crystal structure of...)
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[[Image:2ihf.jpg|left|200px]]<br /><applet load="2ihf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ihf, resolution 1.90&Aring;" />
caption="2ihf, resolution 1.90&Aring;" />
'''Crystal structure of deletion mutant delta 228-252 R190A of the single-stranded DNA binding protein from Thermus aquaticus'''<br />
'''Crystal structure of deletion mutant delta 228-252 R190A of the single-stranded DNA binding protein from Thermus aquaticus'''<br />
==Overview==
==Overview==
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In contrast to the majority of tetrameric SSB proteins, the recently, discovered SSB proteins from the Thermus/Deinoccus group form dimers. We, solved the crystal structures of the SSB protein from Thermus aquaticus, (TaqSSB) and a deletion mutant of the protein and show the structure of, their ssDNA binding domains to be similar to the structure of tetrameric, SSBs. Two conformations accompanied by proline cis-trans isomerization are, observed in the flexible C-terminal region. For the first time, we were, able to trace 6 out of 10 amino acids at the C-terminus of an SSB protein., This highly conserved region is essential for interaction with other, proteins and we show it to adopt an extended conformation devoid of, secondary structure. A model for binding this region to the chi subunit of, DNA polymerase III is proposed. It explains at a molecular level the, reason for the ssb113 phenotype observed in Escherichia coli.
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In contrast to the majority of tetrameric SSB proteins, the recently discovered SSB proteins from the Thermus/Deinoccus group form dimers. We solved the crystal structures of the SSB protein from Thermus aquaticus (TaqSSB) and a deletion mutant of the protein and show the structure of their ssDNA binding domains to be similar to the structure of tetrameric SSBs. Two conformations accompanied by proline cis-trans isomerization are observed in the flexible C-terminal region. For the first time, we were able to trace 6 out of 10 amino acids at the C-terminus of an SSB protein. This highly conserved region is essential for interaction with other proteins and we show it to adopt an extended conformation devoid of secondary structure. A model for binding this region to the chi subunit of DNA polymerase III is proposed. It explains at a molecular level the reason for the ssb113 phenotype observed in Escherichia coli.
==About this Structure==
==About this Structure==
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2IHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IHF OCA].
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2IHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHF OCA].
==Reference==
==Reference==
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[[Category: Curth, U.]]
[[Category: Curth, U.]]
[[Category: Fedorov, R.]]
[[Category: Fedorov, R.]]
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[[Category: Manstein, D.J.]]
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[[Category: Manstein, D J.]]
[[Category: Urbanke, C.]]
[[Category: Urbanke, C.]]
[[Category: Witte, G.]]
[[Category: Witte, G.]]
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[[Category: thermophile organism]]
[[Category: thermophile organism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:19:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:43 2008''

Revision as of 15:52, 21 February 2008


2ihf, resolution 1.90Å

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Crystal structure of deletion mutant delta 228-252 R190A of the single-stranded DNA binding protein from Thermus aquaticus

Overview

In contrast to the majority of tetrameric SSB proteins, the recently discovered SSB proteins from the Thermus/Deinoccus group form dimers. We solved the crystal structures of the SSB protein from Thermus aquaticus (TaqSSB) and a deletion mutant of the protein and show the structure of their ssDNA binding domains to be similar to the structure of tetrameric SSBs. Two conformations accompanied by proline cis-trans isomerization are observed in the flexible C-terminal region. For the first time, we were able to trace 6 out of 10 amino acids at the C-terminus of an SSB protein. This highly conserved region is essential for interaction with other proteins and we show it to adopt an extended conformation devoid of secondary structure. A model for binding this region to the chi subunit of DNA polymerase III is proposed. It explains at a molecular level the reason for the ssb113 phenotype observed in Escherichia coli.

About this Structure

2IHF is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.

Reference

3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins., Fedorov R, Witte G, Urbanke C, Manstein DJ, Curth U, Nucleic Acids Res. 2006;34(22):6708-17. Epub 2006 Dec 5. PMID:17148487

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