A kinase bioscavenger provides antibiotic resistance by extremely tight substrate bindingстатьяЭлектронная публикация
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 12 августа 2020 г.
Аннотация:Microbial communities are self-controlled by repertoires of lethal agents, the antibiotics. In their turn, these antibiotics are regulated by bioscavengers that are selected in the course of evolution. Kinase-mediated phosphorylationrepresents one of the general strategies for the emergence of antibiotic resistance. A new subfamily of AmiN-likekinases, isolated from the Siberian bear microbiome, inactivates antibiotic amicoumacin by phosphorylation. Thenanomolar substrate affinity defines AmiN as a phosphotransferase with a unique catalytic efficiency proximal tothe diffusion limit. Crystallographic analysis and multiscale simulations revealed a catalytically perfect mechanismproviding phosphorylation exclusively in the case of a closed active site that counteracts substrate promiscuity.AmiN kinase is a member of the previously unknown subfamily representing the first evidence of a specializedphosphotransferase bioscavenger.