9LA1
Arabidopsis GORK WT4
Summary for 9LA1
Entry DOI | 10.2210/pdb9la1/pdb |
Related | 9L9U 9LA0 |
EMDB information | 62916 |
Descriptor | Potassium channel GORK (1 entity in total) |
Functional Keywords | outward potassium channel in stomata, plant protein |
Biological source | Arabidopsis thaliana (thale cress) |
Total number of polymer chains | 4 |
Total formula weight | 385637.38 |
Authors | Yamanashi, T.,Kume, T.,Sekido, N.,Muraoka, Y.,Yokoyama, T.,Tanaka, Y.,Uozumi, N. (deposition date: 2025-01-01, release date: 2025-07-16, Last modification date: 2025-08-06) |
Primary citation | Yamanashi, T.,Muraoka, Y.,Furuta, T.,Kume, T.,Sekido, N.,Saito, S.,Terashima, S.,Yokoyama, T.,Tanaka, Y.,Miyamoto, A.,Sato, K.,Ito, T.,Nakazawa, H.,Umetsu, M.,Tanudjaja, E.,Tsujii, M.,Dreyer, I.,Schroeder, J.I.,Ishimaru, Y.,Uozumi, N. Structure reveals a regulation mechanism of plant outward-rectifying K + channel GORK by structural rearrangements in the CNBD-Ankyrin bridge. Proc.Natl.Acad.Sci.USA, 122:e2500070122-e2500070122, 2025 Cited by PubMed Abstract: Guard cells, which regulate stomatal apertures in plants, possess a sophisticated mechanism for regulating turgor pressure. The outward-rectifying "K" channel GORK, expressed in guard cells of the plant , is a central component that promotes stomatal closure by releasing K to the extracellular space, thereby lowering turgor pressure. To date, the structural basis underlying the regulation of the K transport activity of GORK is unclear. Using cryo-EM, we determined the structures of the GORK outward-rectifying K channel with a resolution of 3.16 to 3.27 Å in five distinct conformations that differ significantly in their C-terminal cyclic nucleotide binding domain (CNBD) and ankyrin repeat (ANK) domain. The C-linker connects the transmembrane domains to the C-terminal domains, i.e., CNBD, CNBD-Ankyrin bridge, and ANK. The structural changes and interactions in the C-linker determine whether the closed state of GORK is closer to the preopen state or in a more removed state from the open state of the channel. In particular, interconversion in the short sequence within the CNBD-Ankyrin bridge plays a decisive role in this determination. This region forms an α-helix in the preopened state, while it adopts a nonhelical structure in further distant closed states. The dynamics of the cytosolic region strongly suggest that the K channel activity of GORK is regulated by cytosolic signaling factors during stomatal closure. PubMed: 40699930DOI: 10.1073/pnas.2500070122 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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