Nucleic Acids Research Advance Access originally published online on December 5, 2006
Nucleic Acids Research 2006 34(22):6708-6717; doi:10.1093/nar/gkl1002
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Nucleic Acids Research, 2006, Vol. 34, No. 22 6708-6717
Published by Oxford University Press 2006
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
3D structure of Thermus aquaticus single-stranded DNA–binding protein gives insight into the functioning of SSB proteins
Institute for Biophysical Chemistry, Hannover Medical School Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany
*To whom correspondence should be addressed. Tel: +49 511 532 3707; Fax: + 49 511 532 5966; Email: curth.ute{at}mh-hannover.de
Received July 28, 2006. Revised October 26, 2006. Accepted October 28, 2006.
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 
subunit of DNA polymerase III is proposed. It explains at a molecular level the reason for the ssb113 phenotype observed in Escherichia coli.
Present address: Gregor Witte, Gene Center and Department of Chemistry and Biochemistry, University of Munich (LMU), Feodor-Lynen-Strasse 25, D-81377 Munich, Germany
PDB accession codes: 2ihe and 2ihf
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