Abstract
Gonorrhea infections are becoming more difficult to treat due to the prevalence of strains exhibiting resistance to antibiotics and new therapeutic approaches are needed. N-acetylmuramyl-l-alanine amidase (AmiC) from Neisseria gonorrhoeae is a hydrolase that functions during cell division by cleaving the bond between the N-acetylmuramyl and l-alanine moieties of peptidoglycan. Inhibiting this enzyme offers the prospect of restoring the efficacy of existing antibiotics as treatments against N. gonorrhoeae. Of its two domains, the C-terminal domain catalyses the hydrolysis reaction and the N-terminal domain (NTD) is believed to target AmiC to its peptidoglycan substrate. Here, we report the 1H, 13C, and 15N resonance assignments of a 131 amino acid NTD construct of AmiC by heteronuclear NMR spectroscopy. The assignments represent the first for N. gonorrhoeae AmiC-NTD, laying the groundwork for detailed examination of its structure and dynamics, and providing a platform for new drug discovery efforts to address antimicrobial-resistant N. gonorrhoeae.
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Acknowledgements
This work was supported by the National Institutes of Health (NIH) Award GM066861 (to C.D.). B.Y. was supported by the NIH training award, GM072643.
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The experiments performed comply with the applicable laws of the United States of America and the State of South Carolina.
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Young, B.F., Roth, B.M. & Davies, C. 1H, 13C, and 15N resonance assignments of N-acetylmuramyl-l-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae. Biomol NMR Assign 13, 63–66 (2019). https://doi.org/10.1007/s12104-018-9852-1
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DOI: https://doi.org/10.1007/s12104-018-9852-1