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Lantibiotics: peptides of diverse structure and function.
Annual Review of Microbiology ( IF 10.5 ) Pub Date : 2007-05-18 , DOI: 10.1146/annurev.micro.61.080706.093501
Joanne M Willey 1 , Wilfred A van der Donk
Affiliation  

The current need for antibiotics with novel target molecules has coincided with advances in technical approaches for the structural and functional analysis of the lantibiotics, which are ribosomally synthesized peptides produced by gram-positive bacteria. These peptides have antibiotic or morphogenetic activity and are structurally defined by the presence of unusual amino acids introduced by posttranslational modification. Lantibiotics are complex polycyclic molecules formed by the dehydration of select Ser and Thr residues and the intramolecular addition of Cys thiols to the resulting unsaturated amino acids to form lanthionine and methyllanthionine bridges, respectively. Importantly, the structural and functional diversity of the lantibiotics is much broader than previously imagined. Here we discuss this growing collection of molecules and introduce some recently discovered peptides, review advances in enzymology and protein engineering, and discuss the regulatory networks that govern the synthesis of the lantibiotics by the producing organisms.

中文翻译:

羊毛硫抗生素:具有不同结构和功能的肽。

当前对具有新型靶分子的抗生素的需求与用于羊毛硫抗生素的结构和功能分析的技术方法的进展相吻合,羊毛硫抗生素是由革兰氏阳性细菌产生的核糖体合成的肽。这些肽具有抗生素或形态发生活性,并通过翻译后修饰引入的异常氨基酸在结构上进行定义。羊毛硫抗生素是复杂的多环分子,通过选择的Ser和Thr残基脱水并在分子内将Cys硫醇加到所得的不饱和氨基酸上形成,分别形成羊毛硫氨酸和甲基羊毛硫氨酸桥。重要的是,羊毛硫抗生素的结构和功能多样性比以前想象的要广泛得多。
更新日期:2019-11-01
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