Single particle cryo-EM of KdpFABC WT (KdpB-Ser162-P) in presence of orthovanadate
Ontology highlight
ABSTRACT:
SUBMITTER: Jan Rheinberger
PROVIDER: EMPIAR-11230 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Inhibited KdpFABC transitions into an E1 off-cycle state.
Silberberg Jakob M JM Stock Charlott C Hielkema Lisa L Corey Robin A RA Rheinberger Jan J Wunnicke Dorith D Dubach Victor R A VRA Stansfeld Phillip J PJ Hänelt Inga I Paulino Cristina C
eLife 20221018
KdpFABC is a high-affinity prokaryotic K<sup>+</sup> uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K<sup>+</sup> levels, KdpFABC needs to be inhibited to prevent excessive K<sup>+</sup> accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES<sub>162</sub> motif in the A domain of the pump subunit KdpB (KdpB<sub>S162-P</sub>). Here, we explore the structural basis of in ...[more]
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