Unknown

Dataset Information

0

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


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.

SUBMITTER: Young BF 

PROVIDER: S-EPMC6440844 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N resonance assignments of N-acetylmuramyl-L-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae.

Young Brandon F BF   Roth Braden M BM   Davies Christopher C  

Biomolecular NMR assignments 20181001 1


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. go  ...[more]

Similar Datasets

| S-EPMC1636224 | biostudies-literature
| S-EPMC4865936 | biostudies-literature
| S-EPMC7694207 | biostudies-literature
| S-EPMC5430687 | biostudies-literature
| S-EPMC2927206 | biostudies-literature
| S-EPMC1951811 | biostudies-literature
| S-EPMC2901692 | biostudies-literature
| S-EPMC1223845 | biostudies-other
| S-EPMC3814751 | biostudies-literature
2016-05-24 | GSE73032 | GEO