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Chemical shift assignments of Mb1858 (24-155), a FHA domain-containing protein from Mycobacterium bovis

Overview of attention for article published in Biomolecular NMR Assignments, August 2017
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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.

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This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 September 2017.
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#20,444,703
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