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首页> 外文期刊>Journal of Molecular Biology >Structural and functional characterization of microcin C resistance peptidase MccF from bacillus anthracis
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Structural and functional characterization of microcin C resistance peptidase MccF from bacillus anthracis

机译：炭疽芽孢杆菌对微霉素C的抵抗肽酶MccF的结构和功能表征

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Microcin C (McC) is heptapeptide adenylate antibiotic produced by Escherichia coli strains carrying the mccABCDEF gene cluster encoding enzymes, in addition to the heptapeptide structural gene mccA, necessary for McC biosynthesis and self-immunity of the producing cell. The heptapeptide facilitates McC transport into susceptible cells, where it is processed releasing a non-hydrolyzable aminoacyl adenylate that inhibits an essential aminoacyl-tRNA synthetase. The self-immunity gene mccF encodes a specialized serine peptidase that cleaves an amide bond connecting the peptidyl or aminoacyl moieties of, respectively, intact and processed McC with the nucleotidyl moiety. Most mccF orthologs from organisms other than E. coli are not linked to the McC biosynthesis gene cluster. Here, we show that a protein product of one such gene, MccF from Bacillus anthracis (BaMccF), is able to cleave intact and processed McC, and we present a series of structures of this protein. Structural analysis of apo-BaMccF and its adenosine monophosphate complex reveals specific features of MccF-like peptidases that allow them to interact with substrates containing nucleotidyl moieties. Sequence analyses and phylogenetic reconstructions suggest that several distinct subfamilies form the MccF clade of the large S66 family of bacterial serine peptidases. We show that various representatives of the MccF clade can specifically detoxify non-hydrolyzable aminoacyl adenylates differing in their aminoacyl moieties. We hypothesize that bacterial mccF genes serve as a source of bacterial antibiotic resistance.
机译：Microcin C（McC）是由携带mccABCDEF基因簇编码酶的大肠杆菌菌株产生的七肽腺苷酸抗生素，除了七肽结构基因mccA之外，这是McC生物合成和生产细胞自身免疫所必需的。七肽促进McC转运到易感细胞中，在该细胞中经过加工释放出不可水解的氨酰基腺苷酸，从而抑制了必需的氨酰基tRNA合成酶。自身免疫基因mccF编码一种特殊的丝氨酸肽酶，该酶切割一个酰胺键，该酰胺键分别连接完整的和加工的McC的肽基或氨酰基部分与核苷酸基团。来自除大肠杆菌以外的生物的大多数mccF直系同源物均未与McC生物合成基因簇相关。在这里，我们显示了一个这样的基因，即来自炭疽芽胞杆菌的MccF（BaMccF）的蛋白质产物，能够裂解完整和加工的McC，并且我们展示了该蛋白质的一系列结构。对apo-BaMccF及其单磷酸腺苷复合物的结构分析揭示了MccF样肽酶的特定特征，使它们能够与含有核苷酸基团的底物相互作用。序列分析和系统发育重建表明，几个不同的亚家族构成了细菌丝氨酸肽酶大S66家族的MccF进化枝。我们表明，MccF进化枝的各种代表可以专门解毒在其氨酰基部分不同的不可水解的氨酰基腺苷酸。我们假设细菌的mccF基因可作为细菌对抗生素产生抗药性的来源。

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