Kim, Kook-Han Lee, Won-Kyu Choi, Kyung-Jae Kim, Eunice EunKyeong 2024-01-20T09:00:38Z 2024-01-20T09:00:38Z 2021-09-02 2014-10 1738-2203 https://pubs.kist.re.kr/handle/201004/126320 Bacterial resistance to many existing antibiotics is a growing health concern worldwide. There is an urgent need to identify new antibiotics with unexploited modes of action. Peptide deformylase (PDF) is an essential enzyme involved in N-terminal protein processing in eubacteria but not in higher organisms. Therefore, PDF is considered an attractive target for the development of novel antibiotics. Here, we report the structures of the PDFs from Enterococcus faecalis (EfPDF) and Streptococcus pyogenes (SpyPDF) complexed with actinonin at 1.4 and 2.1 angstrom resolutions, respectively. Actinonin, a naturally occurring, highly potent inhibitor, is bound tightly at the active site. The conformation of actinonin in the EfPDF and SpyPDF complexes was similar to those of all others. The detailed information from this study will facilitate the development of novel antibacterial molecules. English KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY POLYPEPTIDE DEFORMYLASE STAPHYLOCOCCUS-AUREUS DESIGN RESISTANCE INHIBITORS Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes Article 10.1007/s13765-014-4206-x 1 JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.57, no.5, pp.565 - 571 JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY 57 5 565 571 scie scopus kci ART001922276 000345310300005 2-s2.0-84909642791 Food Science & Technology Food Science & Technology Article POLYPEPTIDE DEFORMYLASE STAPHYLOCOCCUS-AUREUS DESIGN RESISTANCE INHIBITORS actinonin antibacterial target drug design Enterococcus faecalis peptide deformylase Streptococcus pyogenes