Biomolecular NMR Assignments

, Volume 13, Issue 1, pp 63–66 | Cite as

1H, 13C, and 15N resonance assignments of N-acetylmuramyl-l-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae

  • Brandon F. Young
  • Braden M. Roth
  • Christopher DaviesEmail author


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.


Neisseria gonorrhoeae Amidase Peptidoglycan metabolism Antibiotic resistance Drug target 



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.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

The experiments performed comply with the applicable laws of the United States of America and the State of South Carolina.


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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyMedical University of South CarolinaCharlestonUSA

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