7T4X
AKT1 K+ channel from A. thaliana in MSP2N2 lipid nanodisc
Summary for 7T4X
| Entry DOI | 10.2210/pdb7t4x/pdb |
| EMDB information | 25691 |
| Descriptor | Potassium channel AKT1, POTASSIUM ION, PHOSPHATIDYLETHANOLAMINE, ... (4 entities in total) |
| Functional Keywords | k+ channel, ion channel, hyperpolarization-activated channel, voltage-gated channel, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 390102.07 |
| Authors | Dickinson, M.S.,Pourmal, S. (deposition date: 2021-12-10, release date: 2021-12-22, Last modification date: 2024-11-06) |
| Primary citation | Dickinson, M.S.,Pourmal, S.,Gupta, M.,Bi, M.,Stroud, R.M. Symmetry Reduction in a Hyperpolarization-Activated Homotetrameric Ion Channel. Biochemistry, 61:2177-2181, 2022 Cited by PubMed Abstract: Plants obtain nutrients from the soil via transmembrane transporters and channels in their root hairs, from which ions radially transport in toward the xylem for distribution across the plant body. We determined structures of the hyperpolarization-activated channel AKT1 from , which mediates K uptake from the soil into plant roots. These structures of AtAKT1 embedded in lipid nanodiscs show that the channel undergoes a reduction of C4 to C2 symmetry, possibly to regulate its electrical activation. PubMed: 34964607DOI: 10.1021/acs.biochem.1c00654 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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