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-Structure paper
| タイトル | A short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of K channel KtrAB. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 4252, Year 2025 |
| 掲載日 | 2025年5月7日 |
著者 | 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 Hänelt / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:40335548 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.82 - 3.56 Å |
| 構造データ | EMDB-14851: KtrAB complex EMDB-14859, PDB-7zpo: EMDB-14862, PDB-7zpr: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-LMT: ![]() ChemComp-K: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / potassium transporter / membrane transport protein / potassium transport / transporter |
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vibrio alginolyticus (バクテリア)
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