- EMDB-61063: Cryo-EM Structure of the Guard Cell Potassium Channel GORK N50 de... -
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基本情報
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データベース: EMDB / ID: EMD-61063
タイトル
Cryo-EM Structure of the Guard Cell Potassium Channel GORK N50 deletion
マップデータ
試料
複合体: GORK N50 deletion
タンパク質・ペプチド: Potassium channel GORK
リガンド: POTASSIUM ION
キーワード
Guard cell / Potassium channel / outward-rectifying / MEMBRANE PROTEIN
機能・相同性
機能・相同性情報
monoatomic ion transmembrane transporter activity / response to jasmonic acid / response to water deprivation / response to abscisic acid / outward rectifier potassium channel activity / monoatomic ion channel complex / monoatomic ion transport / response to cold / response to calcium ion / nucleus 類似検索 - 分子機能
National Natural Science Foundation of China (NSFC)
中国
引用
ジャーナル: Nat Commun / 年: 2025 タイトル: GORK K channel structure and gating vital to informing stomatal engineering. 著者: Xue Zhang / William Carroll / Thu Binh-Anh Nguyen / Thanh-Hao Nguyen / Zhao Yang / Miaolian Ma / Xiaowei Huang / Adrian Hills / Hui Guo / Rucha Karnik / Michael R Blatt / Peng Zhang / 要旨: The Arabidopsis GORK channel is a major pathway for guard cell K efflux that facilitates stomatal closure. GORK is an outwardly-rectifying member of the cyclic-nucleotide binding-homology domain ...The Arabidopsis GORK channel is a major pathway for guard cell K efflux that facilitates stomatal closure. GORK is an outwardly-rectifying member of the cyclic-nucleotide binding-homology domain (CNBHD) family of K channels with close homologues in all other angiosperms known to date. Its bioengineering has demonstrated the potential for enhanced carbon assimilation and water use efficiency. Here we identify critical domains through structural and functional analysis, highlighting conformations that reflect long-lived closed and pre-open states of GORK. These conformations are marked by interactions at the cytosolic face of the membrane between so-called voltage-sensor, C-linker and CNBHD domains, the latter relocating across 10 Å below the voltage sensor. The interactions center around two coupling sites that functional analysis establish are critical for channel gating. The channel is also subject to putative, ligand-like interactions within the CNBHD, which leads to its gating independence of cyclic nucleotides such as cAMP or cGMP. These findings implicate a multi-step mechanism of semi-independent conformational transitions that underlie channel activity and offer promising new sites for optimizing GORK to engineer stomata.