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-13C/15N-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.
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Acknowledgements
We thank for grant supports from Protein Structure Initiative-Biology Program by the National Institute of General Medical Sciences (Grant Nos: U54-GM074958 and U54-GM094597), the “Hundred Talents Program” of Chinese Academy of Sciences, the Ministry of Science and Technology of China (Grant No: 2016YFA051201) and the National Natural Science Foundation of China (Grant No: 21575155).
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He, T., Li, S., Hu, R. et al. Chemical shift assignments of Mb1858 (24-155), a FHA domain-containing protein from Mycobacterium bovis . Biomol NMR Assign 12, 1–4 (2018). https://doi.org/10.1007/s12104-017-9769-0
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DOI: https://doi.org/10.1007/s12104-017-9769-0