3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins.
3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins.
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DOI:
10.1093/nar/gkl1002
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发表时间:
2006
影响因子:
14.9
通讯作者:
Curth, Ute
中科院分区:
文献类型:
--
作者:
Fedorov, Roman;Witte, Gregor;Urbanke, Claus;Manstein, Dietmar J.;Curth, Ute
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 χ 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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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
DOI:
10.1111/j.1432-1033.1991.tb15789.x
发表时间:
1991-02-26
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
作者:
CURTH, U;BAYER, I;MAASS, G
通讯作者:
MAASS, G
影响因子:
2.7
作者:
Matsumoto, T;Morimoto, Y;Yasuoka, N
通讯作者:
Yasuoka, N
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
影响因子:
5.6
作者:
Jones, G;Willett, P;Taylor, R
通讯作者:
Taylor, R