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Related Experiment Video

Updated: Aug 25, 2025

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation
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Inhibited KdpFABC transitions into an E1 off-cycle state.

Jakob M Silberberg1, Charlott Stock1, Lisa Hielkema2

  • 1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Frankfurt, Germany.

Elife
|October 18, 2022
PubMed
Summary

Phosphorylation of KdpB serine 162 inhibits the KdpFABC potassium uptake system by forming a novel E1P tight state. This off-cycle conformation reveals structural insights into P-type ATPase regulation.

Keywords:
E. coliP-type ATPasecryo-EMmembrane transport mechanismmolecular biophysicspotassium uptakeprotein regulationstructural biologystructure–function

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Microbiology

Background:

  • KdpFABC is a prokaryotic potassium (K+) uptake system composed of channel (KdpA) and P-type ATPase (KdpB) subunits.
  • High external K+ necessitates inhibition of KdpFABC to prevent toxic intracellular accumulation.
  • Inhibition is mediated by phosphorylation of KdpB at serine 162 (KdpB_S162-P).

Purpose of the Study:

  • To elucidate the structural mechanisms underlying KdpFABC inhibition by KdpB_S162 phosphorylation.
  • To characterize the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions.

Main Methods:

  • Determination of KdpFABC structures under different functional states.
  • Conformational analysis of the KdpFABC complex.

Main Results:

  • Identification of a novel inhibited state, termed E1P tight, under turnover conditions.
  • The E1P tight state exhibits a compact cytoplasmic domain fold.
  • This state is likely adopted when the transition from E1P to E2P states is blocked.

Conclusions:

  • KdpB_S162 phosphorylation stabilizes an off-cycle E1P tight state, distinct from the canonical Post-Albers cycle.
  • This study provides structural evidence for regulatory off-cycle states in P-type ATPases.
  • The findings contribute to understanding the complex regulation of ion transport systems.