9KHF
AtGORK Full length 1
Summary for 9KHF
| Entry DOI | 10.2210/pdb9khf/pdb |
| EMDB information | 62338 |
| Descriptor | Potassium channel GORK, POTASSIUM ION (2 entities in total) |
| Functional Keywords | complex, transport protein, proton transport |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 350693.88 |
| Authors | |
| Primary citation | Li, Q.Y.,Qin, L.,Tang, L.H.,Zhang, C.R.,Huang, S.,Wang, K.,Zhang, G.H.,Hao, N.J.,Xiao, Q.,Niu, T.,Su, M.,Hedrich, R.,Chen, Y.H. Structural and mechanistic insights into symmetry conversion in plant GORK K+ channel regulation. Protein Cell, 2025 Cited by PubMed Abstract: GORK is a shaker-like potassium channel in plants that contains ankyrin (ANK) repeats. In guard cells, activation of GORK causes K+ efflux, reducing turgor pressure and closing stomata. However, how GORK is regulated remains largely elusive. Here, we solved the cryo-EM structure of Arabidopsis GORK, revealing an unusual symmetry reduction (from C4 to C2) feature within its tetrameric assembly. This symmetry reduction in GORK channel is driven by ANK dimerization, which disrupts the coupling between transmembrane helices and cytoplasmic domains, thus maintaining GORK in an autoinhibited state. Electrophysiological and structural analyses further confirmed that ANK dimerization inhibits GORK, and its removal restores C4 symmetry, converting GORK to an activatable state. This dynamic switching between C2 and C4 symmetry, mediated by ANK dimerization, presents a GORK target site that guard cells regulate to switch the plant K+ channel between inhibited and activatable states, thus controlling stomatal movement in response to environmental stimuli. PubMed: 40996076DOI: 10.1093/procel/pwaf067 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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