2ihe: Difference between revisions

Revision as of 11:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ihe.png

Template:STRUCTURE 2ihe

Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticusCrystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus

Template:ABSTRACT PUBMED 17148487

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus'''
+===Crystal structure of wild-type single-stranded DNA binding protein from Thermus aquaticus===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17148487}}, adds the Publication Abstract to the page
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 [[Category: Protein-protein interaction]]
 [[Category: Thermophile organism]]
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