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A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperoneстатья
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: 3 декабря 2017 г.
- Авторы: Holdbrook Daniel A., Burmann Bjorn M., Huber Roland G., Petoukhov Maxim V., Svergun Dmitri I., Hiller Sebastian, Bond Peter J.
- Журнал: Structure
- Том: 25
- Номер: 7
- Год издания: 2017
- Издательство: Cell Press
- Местоположение издательства: United States
- Первая страница: 1079
- DOI: 10.1016/j.str.2017.05.018
- Аннотация: The trimeric periplasmic holdase chaperone Skp binds and stabilizes unfolded outer membrane proteins (OMPs) as part of bacterial OMP biogenesis. Skp binds client proteins in its central cavity, thereby reducing its backbone dynamics, but the molecular mechanisms that govern Skp dynamics and adaptation to differently sized clients remains unknown. Here, we employ a combination of microsecond time-scale molecular dynamics simulation, small-angle X-ray scattering, and nuclear magnetic resonance spectroscopy to reveal that Skp is remarkably flexible, and features a molecular spring-loaded mechanism in its “tentacle” arms that enables switching between two distinct conformations on sub-millisecond timescales. The conformational switch is executed around a conserved pivot element within the coiled-coil structures of the tentacles, allowing expansion of the cavity and thus accommodation of differently sized clients. The spring-loaded mechanism shows how a chaperone can efficiently modulate its structure and function in an ATP-independent manner.
- Добавил в систему: Петухов Максим Владимирович