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TitleCryo-EM structures of Arabidopsis CNGC1 and CNGC5 reveal molecular mechanisms underlying gating and calcium selectivity.
Journal, issue, pagesNat Plants, Vol. 11, Issue 3, Page 632-642, Year 2025
Publish dateFeb 20, 2025
AuthorsJianping Wang / Bo-Ya Du / Xue Zhang / Xiaomin Qu / Yang Yang / Zhao Yang / Yong-Fei Wang / Peng Zhang /
PubMed AbstractPlant cyclic nucleotide-gated channels (CNGCs) belong to the cyclic nucleotide-binding domain (CNBD) channel family, but are phylogenetically classified in a distinct branch. In contrast to their ...Plant cyclic nucleotide-gated channels (CNGCs) belong to the cyclic nucleotide-binding domain (CNBD) channel family, but are phylogenetically classified in a distinct branch. In contrast to their animal counterparts of K-selective or non-selective cation channels, plant CNGCs mainly mediate Ca influx and are involved in various physiological processes, such as stomatal movements, pollen-tube growth and immune responses. Here, we present the cryo-EM structure and electrophysiological analysis of plant CNGC representatives, Arabidopsis CNGC1 and CNGC5. We found that CNGC1 and CNGC5 contain a unique extracellular domain featuring disulfide bonds that is essential for channel gating via coupling of the voltage-sensing domain with the pore domain. The pore domain selectivity filter possesses a Gln residue at the constriction site that determines the Ca selectivity. Replacement of this Gln with Glu, typically observed in CNBD-type non-selective cation channels, could convert CNGC1 and CNGC5 from Ca-selective channels to non-selective cation channels permeable to Ca, Na or K. In addition, we found that the CNGC1 and CNGC5 CNBD homology domain contains intrinsic-ligand-like interactions, which may devoid the binding of cyclic nucleotides and lead to gating independent of cAMP or cGMP. This research not only provides a mechanistic understanding of plant CNGCs' function, but also adds to the comprehensive knowledge of the CNBD channels.
External linksNat Plants / PubMed:39979428
MethodsEM (single particle)
Resolution2.5 - 2.71 Å
Structure data

61105

9j34

EMDB-61105, PDB-9j34:
Cryo-EM structure of Arabidopsis CNGC1
Method: EM (single particle) / Resolution: 2.51 Å

61106

9j35

EMDB-61106, PDB-9j35:
Cryo-EM structure of Arabidopsis CNGC5 in nanodisc
Method: EM (single particle) / Resolution: 2.71 Å

61107

9j36

EMDB-61107, PDB-9j36:
Cryo-EM structure of Arabidopsis CNGC5
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsPLANT PROTEIN / Cryo-EM / Membrane protein / polymer

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