Structure of the single-stranded DNA-binding protein SSB from Thermus aquaticus

被引：19
|
作者：
Jedrzejczak, Robert
Dauter, Miroslawa
Dauter, Zbigniew [1 ]
Olszewski, Marcin
Dlugolecka, Anna
Kur, Jozef
机构：
[1] NCI, Synchrotron Radiat Res Sect, MCL, Argonne Natl Lab, Argonne, IL 60439 USA
[2] Argonne Natl Lab, Basic Res Program, SAIC Frederick, Argonne, IL 60439 USA
[3] Gdansk Univ Technol, Fac Chem, Dept Microbiol, PL-80952 Gdansk, Poland
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2006年 / 62卷
关键词：
D O I：
10.1107/S0907444906036031
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The crystal structure of the single-stranded DNA-binding protein from Thermus aquaticus has been solved and refined at 1.85 angstrom resolution. Two monomers, each encompassing two oligonucleotide/oligosaccharide-binding (OB) domains and a number of flexible beta-hairpin loops, form an oligomer of approximate D-2 symmetry typical of bacterial SSBs. Comparison with other SSB structures confirms considerable variability in the mode of oligomerization and aggregation of SSB oligomers.
引用
收藏
页码：1407 / 1412
页数：6
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