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首页> 外文期刊>Journal of the Korean Society for Applied Biological Chemistry >Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes
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Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes

机译：粪肠球菌和化脓性链球菌的肌动蛋白结合肽脱甲酰酶的结构

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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
机译：对许多现有抗生素的细菌耐药性在世界范围内日益引起人们的健康关注。迫切需要鉴定具有未开发作用方式的新抗生素。肽去甲酰基化酶（PDF）是一种在真细菌中参与N端蛋白质加工的必需酶，但在高等生物中却不参与。因此，PDF被认为是开发新型抗生素的有吸引力的目标。在这里，我们报告粪便肠球菌（EfPDF）和化脓性链球菌（SpyPDF）与肌动蛋白复合在1.4和2.1埃分辨率分别PDF的结构。肌动蛋白是一种天然存在的高效抑制剂，在活性部位紧密结合。 EfPDF和SpyPDF复合物中肌动蛋白的构象与其他所有构象相似。这项研究的详细信息将促进新型抗菌分子的开发

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