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Structure paper

TitleA short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of K channel KtrAB.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 4252, Year 2025
Publish dateMay 7, 2025
AuthorsJanina Stautz / David Griwatz / Susann Kaltwasser / Ahmad Reza Mehdipour / Sophie Ketter / Celina Thiel / Dorith Wunnicke / Marina Schrecker / Deryck J Mills / Gerhard Hummer / Janet Vonck / Inga Hänelt /
PubMed AbstractK 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 ...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.
External linksNat Commun / PubMed:40335548 / PubMed Central
MethodsEM (single particle)
Resolution2.82 - 3.56 Å
Structure data

14851

7zp9

EMDB-14851: KtrAB complex
PDB-7zp9: KtrAB complex - KtrA8 ring with a KtrB dimer on each side
Method: EM (single particle) / Resolution: 2.82 Å

14859

7zpo

EMDB-14859, PDB-7zpo:
native KtrAB complex
Method: EM (single particle) / Resolution: 3.24 Å

14862

7zpr

EMDB-14862, PDB-7zpr:
KtrAB complex with N-terminal deletion of KtrB 1-19
Method: EM (single particle) / Resolution: 3.56 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • vibrio alginolyticus (bacteria)
KeywordsMEMBRANE PROTEIN / potassium transporter / membrane transport protein / potassium transport / transporter

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