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TitleGORK K channel structure and gating vital to informing stomatal engineering.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1961, Year 2025
Publish dateFeb 25, 2025
AuthorsXue 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 /
PubMed AbstractThe 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.
External linksNat Commun / PubMed:40000640 / PubMed Central
MethodsEM (single particle)
Resolution2.43 - 3.14 Å
Structure data

EMDB-61061, PDB-9j0x:
Cryo-EM Structure of the Guard Cell Potassium Channel GORK
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-61062, PDB-9j0y:
Cryo-EM Structure of the Guard Cell Potassium Channel GORK mutant
Method: EM (single particle) / Resolution: 3.14 Å

EMDB-61063, PDB-9j0z:
Cryo-EM Structure of the Guard Cell Potassium Channel GORK N50 deletion
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-61064, PDB-9j10:
Cryo-EM Structure of the Guard Cell Potassium Channel GORK N23 deletion
Method: EM (single particle) / Resolution: 2.43 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / Guard cell / Potassium channel / outward-rectifying

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