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Single particle cryo-EM of KdpFABC WT (KdpB-Ser162-P) under turnover condition

ABSTRACT:

SUBMITTER: Jan Rheinberger

PROVIDER: EMPIAR-11232 | biostudies-other |

REPOSITORIES: biostudies-other

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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+ uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K+ levels, KdpFABC needs to be inhibited to prevent excessive K+ accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES162 motif in the A domain of the pump subunit KdpB (KdpBS162-P). Here, we explore the structural basis of in ...[more]

PMID: 36255052

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