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.
复制标题

DOI:
10.1093/nar/gkl1002
复制
发表时间:
2006
影响因子:
14.9
通讯作者:
Curth, Ute
Curth, Ute
中科院分区:
生物学2区
文献类型:
--
作者:
Fedorov, Roman;Witte, Gregor;Urbanke, Claus;Manstein, Dietmar J.;Curth, Ute

文献摘要

参考文献

被引文献

相似文献

与大多数四聚体SSB蛋白相反,最近发现的来自Thermus/Deinoccus组的SSB蛋白形成二聚体。我们解决了SSB蛋白质的晶体结构从Thermus aquaticus(TaqSSB)和蛋白质的缺失突变体,并显示其ssDNA结合结构域的结构类似于四聚体SSB的结构。在柔性C-末端区域观察到两种构象伴随脯氨酸顺反异构化。这是第一次,我们能够追踪SSB蛋白C-末端10个氨基酸中的6个。这个高度保守的区域是必不可少的与其他蛋白质的相互作用,我们表明,它采取了扩展的构象缺乏二级结构。提出了一个结合该区域的DNA聚合酶III的χ亚基的模型。它在分子水平上解释了在大肠杆菌中观察到ssb 113表型的原因。
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.
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
DOI: 10.1093/oxfordjournals.jbchem.a022611
发表时间: 2000-02-01
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
DOI: 10.1006/jmbi.1996.0897
发表时间: 1997-04-04
影响因子: 5.6
作者:
Jones, G;Willett, P;Taylor, R
通讯作者: Taylor, R