Open biology · 2025
Structure of WzxE the lipid III flippase for Enterobacterial Common Antigen polysaccharide.
СтатьяНазвание и аннотация: Перевод в очереди
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Le Bas Audrey, Clarke Bradley R, Teelucksingh Tanisha, Lee Micah, El Omari Kamel, Giltrap Andrew M, McMahon Stephen A, Liu Hui, Beale John H, Mykhaylyk Vitaliy, Duman Ramona, Paterson Neil G, Ward Philip N, Harrison Peter J, Weckener Miriam, Pardon Els, Steyaert Jan, Liu Huanting, Quigley Andrew, Davis Benjamin G, Wagner Armin, Whitfield Chris, Naismith James H
Аннотация
The enterobacterial common antigen (ECA) is conserved in Gram-negative bacteria of the Enterobacterales order although its function is debated. ECA biogenesis depends on the Wzx/Wzy-dependent strategy whereby the newly synthesized lipid-linked repeat units, lipid III, are transferred across the inner membrane by the lipid III flippase WzxE. WzxE is part of the Wzx family and required in many glycan assembly systems, but an understanding of its molecular mechanism is hindered due to a lack of structural evidence. Here, we present the first X-ray structures of WzxE from Escherichia coli in complex with nanobodies. Both inward- and outward-facing conformations highlight two pairs of arginine residues that move in a reciprocal fashion, enabling flipping. One of the arginine pairs coordinated to a glutamate residue is essential for activity along with the C-terminal arginine rich tail located close to the entrance of the lumen. This work helps understand the translocation mechanism of the Wzx flippase family.