Chemical shift assignments of the homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae.
Chemical shift assignments of the homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae.
复制标题
肺炎链球菌同源二聚体蛋白 SP_0782 (7-79) 的化学位移分配。
DOI：
10.1007/s12104-016-9697-4
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发表时间：
2016
影响因子：
0.9
通讯作者：
Yang Yunhuang
中科院分区：
文献类型：
--
作者：
Li Shuangli;Ramelot Theresa A;Kennedy Michael A;Liu Maili;Yang Yunhuang
肺炎链球菌（Streptococcus pneumoniae）的SP_0782蛋白是一个小的同源二聚体蛋白，属于具有单链DNA（single-stranded DNA，ssDNA）结合功能的蛋白家族。以前的特点是结合到一个20聚体的富含吡啶的ssDNA，共享一个整体类似的结构折叠与人类转录辅激活因子PC4的同源YdbC从乳酸乳球菌的ssDNA结合。我们报告说，SP_0782表现出明显的差异，从YdbC的ssDNA结合性能所揭示的NMR滴定实验。与ssDNA dT19G1与PC4和YdbC的结合不同，SP_0782导致聚集。此外，SP_0782表现出与较短ssDNA如dT6的有利结合。原因尚不清楚，SP_0782的结构-功能关系仍有待阐明。在这里，我们报告了SP_0782残基7 - 79的完整1H、13C和15N主链和侧链NMR归属。
The protein SP_0782 fromStreptococcus pneumoniais a small homodimeric protein that belongs to a protein family containing representative members with single-stranded DNA (ssDNA) binding functions. The ssDNA binding of the homolog YdbC fromLactococcus lactiswas previously characterized when bound to a 20-mer of pyridine-rich ssDNA, sharing an overall similar structural fold with the human transcription coactivator PC4. We report that SP_0782 exhibits distinct differences in ssDNA binding properties from YdbC as revealed by NMR titration experiments. Unlike the binding of the ssDNA dT19G1 to PC4 and YdbC, SP_0782 resulted in aggregation. In addition, SP_0782 exhibits favorable binding to shorter ssDNA such as dT6. The reason is unclear, and the SP_0782 structure–function relationship remains to be elucidated. Here, we report the complete1H,13C, and15N backbone and side chain NMR assignments of SP_0782, residues 7–79.