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Inhibited KdpFABC transitions into an E1 off-cycle state
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Silberberg, Jakob M., Stock, Charlott, Hielkema, Lisa, Corey, Robin A., Rheinberger, Jan, Wunnicke, Dorith, Dubach, Victor R. A., Stansfeld, Phillip J., Hänelt, Inga and Paulino, Cristina (2022) Inhibited KdpFABC transitions into an E1 off-cycle state. eLife, 11 . doi:10.7554/elife.80988 ISSN 2050-084X.
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Official URL: https://doi.org/10.7554/elife.80988
Abstract
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 inhibition by KdpBS162 phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC state that we termed E1P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1P state adopted by KdpFABC upon KdpBS162 phosphorylation. The E1P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1P states to E2P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such states.
Item Type: | Journal Article | |||||||||||||||||||||||||||||||||||||||
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Subjects: | Q Science > QD Chemistry Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) Faculty of Science, Engineering and Medicine > Science > Chemistry > Computational and Theoretical Chemistry Centre |
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SWORD Depositor: | Library Publications Router | |||||||||||||||||||||||||||||||||||||||
Library of Congress Subject Headings (LCSH): | Prokaryotes , Prokaryotes -- Physiology, Phosphorylation | |||||||||||||||||||||||||||||||||||||||
Journal or Publication Title: | eLife | |||||||||||||||||||||||||||||||||||||||
Publisher: | eLife Sciences Publications, Ltd | |||||||||||||||||||||||||||||||||||||||
ISSN: | 2050-084X | |||||||||||||||||||||||||||||||||||||||
Official Date: | 18 October 2022 | |||||||||||||||||||||||||||||||||||||||
Dates: |
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Volume: | 11 | |||||||||||||||||||||||||||||||||||||||
DOI: | 10.7554/elife.80988 | |||||||||||||||||||||||||||||||||||||||
Status: | Peer Reviewed | |||||||||||||||||||||||||||||||||||||||
Publication Status: | Published | |||||||||||||||||||||||||||||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||||||||||||||||||||
Date of first compliant deposit: | 21 November 2022 | |||||||||||||||||||||||||||||||||||||||
Date of first compliant Open Access: | 22 November 2022 | |||||||||||||||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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