2ihf
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Crystal structure of deletion mutant delta 228-252 R190A of the 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
2IHF 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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