Author
Listed:
- Janina Stautz
(Goethe University Frankfurt)
- David Griwatz
(Goethe University Frankfurt)
- Susann Kaltwasser
(Max Planck Institute of Biophysics)
- Ahmad Reza Mehdipour
(Ghent University
Max Planck Institute of Biophysics)
- Sophie Ketter
(Goethe University Frankfurt)
- Celina Thiel
(Goethe University Frankfurt)
- Dorith Wunnicke
(Goethe University Frankfurt)
- Marina Schrecker
(Goethe University Frankfurt)
- Deryck J. Mills
(Max Planck Institute of Biophysics)
- Gerhard Hummer
(Max Planck Institute of Biophysics
Goethe University Frankfurt)
- Janet Vonck
(Max Planck Institute of Biophysics)
- Inga Hänelt
(Goethe University Frankfurt)
Abstract
K+ homeostasis is crucial for bacterial survival. The bacterial K+ channel KtrAB is regulated by the binding of ADP and ATP to the cytosolic RCK subunits KtrA. While the ligand-induced conformational changes in KtrA are well described, the transmission to the gating regions within KtrB is not understood. Here, we present a cryo-EM structure of the ADP-bound, inactive KtrAB complex from Vibrio alginolyticus, which resolves part of KtrB’s N termini. They are short intrinsically disordered regions (IDRs) located at the interface of KtrA and KtrB. We reveal that these IDRs play a decisive role in ATP-mediated channel opening, while the closed ADP-bound state does not depend on the N-termini. We propose an allosteric mechanism, in which ATP-induced conformational changes within KtrA trigger an interaction of KtrB’s N-terminal IDRs with the membrane, stabilizing the active and conductive state of KtrAB.
Suggested Citation
Janina Stautz & David Griwatz & Susann Kaltwasser & Ahmad Reza Mehdipour & Sophie Ketter & Celina Thiel & Dorith Wunnicke & Marina Schrecker & Deryck J. Mills & Gerhard Hummer & Janet Vonck & Inga Hän, 2025.
"A short intrinsically disordered region at KtrB’s N-terminus facilitates allosteric regulation of K+ channel KtrAB,"
Nature Communications, Nature, vol. 16(1), pages 1-16, December.
Handle:
RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59546-z
DOI: 10.1038/s41467-025-59546-z
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