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Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibitionстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Travin D.Y., Watson Z.L., Metelev M., Ward F.R., Osterman I.A., Khven I.M., Khabibullina N.F., Serebryakova M., Mergaert P., Polikanov Y.S., Cate J.H.D, Severinov K.
- Журнал: Nature communications
- Том: 10
- Номер: 4563
- Год издания: 2019
- Издательство: Nature Pub. Group
- Местоположение издательства: United Kingdom
- DOI: 10.1038/s41467-019-12589-5
- Аннотация: Ribosome-synthesized post-translationally modified peptides (RiPPs) represent a rapidly expanding class of natural products with various biological activities. Linear azol(in)e-containing peptides (LAPs) comprise a subclass of RiPPs that display outstanding diversity of mechanisms of action while sharing common structural features. Here, we report the discovery of a new LAP biosynthetic gene cluster in the genome of Rhizobium Pop5, which encodes the precursor peptide and modification machinery of phazolicin (PHZ) – an extensively modified peptide exhibiting narrow-spectrum antibacterial activity against some symbiotic bacteria of leguminous plants. The cryo-EM structure of the Escherichia coli 70S-PHZ complex reveals that the drug interacts with the 23S rRNA and uL4/uL22 proteins and obstructs ribosomal exit tunnel in a way that is distinct from other compounds. We show that the uL4 loop sequence determines the species-specificity of antibiotic action. PHZ expands the known diversity of LAPs and may be used in the future as biocontrol agent for agricultural needs.
- Добавил в систему: Травин Дмитрий Юрьевич
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | 2019_Travin_et_al._PHZ.pdf | 3,1 МБ | 29 октября 2019 [travin] |