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Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC
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Silberberg, Jakob M., Corey, Robin A., Hielkema, Lisa, Stock, Charlott, Stansfeld, Phillip J., Paulino, Cristina and Hänelt, Inga (2021) Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC. Nature Communications, 12 (1). 5098. doi:10.1038/s41467-021-25242-x ISSN 2041-1723.
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Official URL: http://dx.doi.org/10.1038/s41467-021-25242-x
Abstract
KdpFABC, a high-affinity K+ pump, combines the ion channel KdpA and the P-type ATPase KdpB to secure survival at K+ limitation. Here, we apply a combination of cryo-EM, biochemical assays, and MD simulations to illuminate the mechanisms underlying transport and the coupling to ATP hydrolysis. We show that ions are transported via an intersubunit tunnel through KdpA and KdpB. At the subunit interface, the tunnel is constricted by a phenylalanine, which, by polarized cation-π stacking, controls K+ entry into the canonical substrate binding site (CBS) of KdpB. Within the CBS, ATPase coupling is mediated by the charge distribution between an aspartate and a lysine. Interestingly, individual elements of the ion translocation mechanism of KdpFABC identified here are conserved among a wide variety of P-type ATPases from different families. This leads us to the hypothesis that KdpB might represent an early descendant of a common ancestor of cation pumps.
Item Type: | Journal Article | |||||||||||||||||||||||||||||||||||||||
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Subjects: | Q Science > QC Physics Q Science > QD Chemistry Q Science > QP Physiology |
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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): | Transport theory, Ion flow dynamics, Adenosine triphosphatase, Hydrolysis | |||||||||||||||||||||||||||||||||||||||
Journal or Publication Title: | Nature Communications | |||||||||||||||||||||||||||||||||||||||
Publisher: | Nature Publishing Group | |||||||||||||||||||||||||||||||||||||||
ISSN: | 2041-1723 | |||||||||||||||||||||||||||||||||||||||
Official Date: | 24 August 2021 | |||||||||||||||||||||||||||||||||||||||
Dates: |
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Volume: | 12 | |||||||||||||||||||||||||||||||||||||||
Number: | 1 | |||||||||||||||||||||||||||||||||||||||
Article Number: | 5098 | |||||||||||||||||||||||||||||||||||||||
DOI: | 10.1038/s41467-021-25242-x | |||||||||||||||||||||||||||||||||||||||
Status: | Peer Reviewed | |||||||||||||||||||||||||||||||||||||||
Publication Status: | Published | |||||||||||||||||||||||||||||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||||||||||||||||||||
Date of first compliant deposit: | 16 September 2021 | |||||||||||||||||||||||||||||||||||||||
Date of first compliant Open Access: | 20 September 2021 | |||||||||||||||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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