Inhibited KdpFABC resides in an E1 off-cycle state
Jakob M. Silberberg, Charlott Stock, Lisa Hielkema, Robin Adam Corey, Jan Rheinberger, Dorith Wunnicke, Victor R. A. Dubach, Phillip James Stansfeld, Inga Hänelt, Cristina Paulino
This study identifies a new inhibited conformation of KdpFABC, termed E1-P tight, resulting from KdpBS162 phosphorylation, which represents an off-cycle state in P-type ATPases.
eLife · Oct 18, 2022Peer-reviewedMolecular Biology