Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843

被引:1
|
作者
Haikarainen, Teemu [1 ,2 ]
Loimaranta, Vuokko [3 ]
Prieto-Lopez, Carlos [1 ,2 ]
Battula, Pradeep [1 ,2 ]
Finne, Jukka [4 ]
Papageorgiou, Anastassios C. [1 ,2 ]
机构
[1] Univ Turku, Turku Ctr Biotechnol, Turku 20521, Finland
[2] Abo Akad Univ, Turku 20521, Finland
[3] Univ Turku, Dept Med Biochem & Genet, FIN-20520 Turku, Finland
[4] Univ Helsinki, Dept Biosci, FIN-00014 Helsinki, Finland
基金
芬兰科学院;
关键词
RECOGNITION; PHASE;
D O I
10.1107/S1744309113009664
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 angstrom resolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I4(1), with unit-cell parameters a = b = 121.4, c = 51.5 angstrom and one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.
引用
收藏
页码:559 / 561
页数:3
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