Download MendeleyThe gating cycle of a K+ channel at atomic resolution.
Cuello, L.G., Cortes, D.M., Perozo, E.(2017) Elife 6
- PubMed: 29165243
- DOI: https://doi.org/10.7554/eLife.28032
- Primary Citation of Related Structures:
5VK6, 5VKE, 5VKH - PubMed Abstract:
C-type inactivation in potassium channels helps fine-tune long-term channel activity through conformational changes at the selectivity filter. Here, through the use of cross-linked constitutively open constructs, we determined the structures of KcsA's mutants that stabilize the selectivity filter in its conductive (E71A, at 2.25 ?) and deep C-type inactivated (Y82A at 2.4 ?) conformations. These structural snapshots represent KcsA's transient open-conductive (O/O) and the stable open deep C-type inactivated states (O/I), respectively. The present structures provide an unprecedented view of the selectivity filter backbone in its collapsed deep C-type inactivated conformation, highlighting the close interactions with structural waters and the local allosteric interactions that couple activation and inactivation gating. Together with the structures associated with the closed-inactivated state (C/I) and in the well-known closed conductive state (C/O), this work recapitulates, at atomic resolution, the key conformational changes of a potassium channel pore domain as it progresses along its gating cycle.
Organizational Affiliation:
Center for Membrane Protein Research, Department of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, United States.
