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Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poisonстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 22 февраля 2019 г.
- Авторы: Ghilarov Dmitry, Stevenson Clare E.M., Travin Dmitrii Y., Piskunova Julia, Serebryakova Marina, Maxwell Anthony, Lawson David M., Severinov Konstantin
- Журнал: Molecular Cell
- Том: 73
- Номер: 4
- Год издания: 2019
- Издательство: Cell Press
- Местоположение издательства: United States
- Первая страница: 749
- Последняя страница: 762
- DOI: 10.1016/j.molcel.2018.11.032
- Аннотация: The introduction of azole heterocycles into a peptide backbone is the principal step in the biosynthesis of numerous compounds with therapeutic potential. One of them is microcin B17, a bacterial topoisomerase inhibitor whose activity depends on the conversion of selected serine and cysteine residues of the precursor peptide to oxazoles and thiazoles by the McbBCD synthetase complex. Crystal structures of McbBCD reveal an octameric BCD complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer. An atomic-level view of the azole synthetase is a starting point for deeper understanding and control of biosynthesis of a large group of ribosomally synthesized natural products.
- Добавил в систему: Серебрякова Марина Васильевна