Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by x-ray structure analysis

被引:56
作者
Matsumoto, T
Morimoto, Y
Shibata, N
Kinebuchi, T
Shimamoto, N
Tsukihara, T
Yasuoka, N
机构
[1] Himeji Inst Technol, Dept Life Sci, Kamigori, Hyogo 6781297, Japan
[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
[3] Natl Inst Genet, Struct Biol Ctr, Mishima, Shizuoka 4118540, Japan
关键词
crystal structure analysis; positive concavity; single-stranded DNA binding protein;
D O I
10.1093/oxfordjournals.jbchem.a022611
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The single-stranded DNA (ssDNA) binding protein from Escherichia coli (EcoSSB) plays a central role in DNA replication, recombination, and repair: The tertiary structure of EcoSSB was determined at 2.2 Angstrom resolution. This is rather higher resolution than previously reported. Crystals were grown from the homogeneous intact protein but the EcoSSB tetramer in the crystals contains truncated subunits lacking a part of the C-terminal, The structure determined includes biologically important flexible loops and C-terminal regions, and revealed the existence of concavities. These concavities include the residues important for ssDNA binding. An ssDNA can be fitted on the concavities and further stabilized through interactions with the loops forming flexible lids. It seems likely to play a central role in the binding of ssDNA.
引用
收藏
页码:329 / 335
页数:7
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