Title |
Chemical shift assignments of Mb1858 (24-155), a FHA domain-containing protein from Mycobacterium bovis
|
---|---|
Published in |
Biomolecular NMR Assignments, August 2017
|
DOI | 10.1007/s12104-017-9769-0 |
Pubmed ID | |
Authors |
Ting He, Shuangli Li, Rui Hu, Theresa A. Ramelot, Michael A. Kennedy, Yunhuang Yang, Jiang Zhu, Maili Liu |
Abstract |
The forkhead-associated (FHA) domain is known as a phosphopeptide recognition domain embedded in regulatory proteins from both eukaryotes and bacteria with various biological functions. In this study, the gene encoding a predicted FHA domain from Mb1858 (residues V24-D155 from the 162 amino acid protein Mb1858) in Mycobacterium bovis was cloned, and U-(13)C/(15)N-labeled protein was prepared for backbone and side chain resonance assignments by NMR spectroscopy. These assignments are preliminary work towards the determination of the structure and phosphopeptide-binding properties using NMR methods, which will provide useful information about the function of Mb1858 protein. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
United Kingdom | 1 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 1 | 100% |