8TEO
Shaker in low K+ (4mM K+)
Summary for 8TEO
| Entry DOI | 10.2210/pdb8teo/pdb |
| EMDB information | 41193 |
| Descriptor | Potassium voltage-gated channel protein Shaker, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | voltage-gated potassium channel, membrane protein |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 4 |
| Total formula weight | 322504.44 |
| Authors | |
| Primary citation | Stix, R.,Tan, X.F.,Bae, C.,Fernandez-Marino, A.I.,Swartz, K.J.,Faraldo-Gomez, J.D. Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse. Sci Adv, 9:eadj5539-eadj5539, 2023 Cited by PubMed Abstract: Eukaryotic voltage-gated K channels have been extensively studied, but the structural bases for some of their most salient functional features remain to be established. C-type inactivation, for example, is an auto-inhibitory mechanism that confers temporal resolution to their signal-firing activity. In a recent breakthrough, studies of a mutant of Shaker that is prone to inactivate indicated that this process entails a dilation of the selectivity filter, the narrowest part of the ion conduction pathway. Here, we report an atomic-resolution cryo-electron microscopy structure that demonstrates that the wild-type channel can also adopt this dilated state. All-atom simulations corroborate this conformation is congruent with the electrophysiological characteristics of the C-type inactivated state, namely, residual K conductance and altered ion specificity, and help rationalize why inactivation is accelerated or impeded by certain mutations. In summary, this study establishes the molecular basis for an important self-regulatory mechanism in eukaryotic K channels, laying a solid foundation for further studies. PubMed: 38064553DOI: 10.1126/sciadv.adj5539 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.39 Å) |
Structure validation
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