2ihe: Difference between revisions
New page: left|200px<br /><applet load="2ihe" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihe, resolution 2.10Å" /> '''Crystal structure of... |
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[[Image:2ihe.jpg|left|200px]]<br /><applet load="2ihe" size=" | [[Image:2ihe.jpg|left|200px]]<br /><applet load="2ihe" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ihe, resolution 2.10Å" /> | caption="2ihe, resolution 2.10Å" /> | ||
'''Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus'''<br /> | '''Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus'''<br /> | ||
==Overview== | ==Overview== | ||
In contrast to the majority of tetrameric SSB proteins, the recently | 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== | ||
2IHE 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:// | 2IHE 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=2IHE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Curth, U.]] | [[Category: Curth, U.]] | ||
[[Category: Fedorov, R.]] | [[Category: Fedorov, R.]] | ||
[[Category: Manstein, D | [[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]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:45 2008'' | ||
Revision as of 18:52, 21 February 2008
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Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus
OverviewOverview
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 StructureAbout this Structure
2IHE is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
ReferenceReference
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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