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Open data
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Basic information
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Title | Cryo-EM structure of Arabidopsis CNGC1 | |||||||||
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![]() | Cryo-EM / Membrane protein / polymer / PLANT PROTEIN | |||||||||
Function / homology | ![]() monoatomic ion channel activity / cGMP binding / cAMP binding / calmodulin binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.51 Å | |||||||||
![]() | Wang JP / Zhang P / Zhang X | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of Arabidopsis CNGC1 and CNGC5 reveal molecular mechanisms underlying gating and calcium selectivity. Authors: Jianping Wang / Bo-Ya Du / Xue Zhang / Xiaomin Qu / Yang Yang / Zhao Yang / Yong-Fei Wang / Peng Zhang / ![]() Abstract: 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 ...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. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 167.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.1 KB 20.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.8 KB | Display | ![]() |
Images | ![]() | 136.8 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() | 164.9 MB 164.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 780.6 KB | Display | ![]() |
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Full document | ![]() | 780.1 KB | Display | |
Data in XML | ![]() | 20.3 KB | Display | |
Data in CIF | ![]() | 26 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9j34MC ![]() 9j35C ![]() 9j36C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.932 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
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Density Histograms |
-Half map: #1
File | emd_61105_half_map_2.map | ||||||||||||
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Sample components
-Entire : Structure of CNGC1 in GDN
Entire | Name: Structure of CNGC1 in GDN |
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Components |
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-Supramolecule #1: Structure of CNGC1 in GDN
Supramolecule | Name: Structure of CNGC1 in GDN / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Cyclic nucleotide-gated ion channel 1
Macromolecule | Name: Cyclic nucleotide-gated ion channel 1 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 83.203141 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MNFRQEKFVR FQDWKSDKTS SDVEYSGKNE IQTGIFQRTI SSISDKFYRS FESSSARIKL FKRSYKSYSF KEAVSKGIGS THKILDPQG PFLQRWNKIF VLACIIAVSL DPLFFYVPII DDAKKCLGID KKMEITASVL RSFTDVFYVL HIIFQFRTGF I APSSRVFG ...String: MNFRQEKFVR FQDWKSDKTS SDVEYSGKNE IQTGIFQRTI SSISDKFYRS FESSSARIKL FKRSYKSYSF KEAVSKGIGS THKILDPQG PFLQRWNKIF VLACIIAVSL DPLFFYVPII DDAKKCLGID KKMEITASVL RSFTDVFYVL HIIFQFRTGF I APSSRVFG RGVLVEDKRE IAKRYLSSHF IIDILAVLPL PQMVILIIIP HMRGSSSLNT KNMLKFIVFF QYIPRFIRIY PL YKEVTRT SGILTETAWA GAAFNLFLYM LASHVFGAFW YLFSIERETV CWKQACERNN PPCISKLLYC DPETAGGNAF LNE SCPIQT PNTTLFDFGI FLDALQSGVV ESQDFPQKFF YCFWWGLQNL SSLGQNLKTS TYIWEICFAV FISIAGLVLF SFLI GNMQT YLQSTTTRLE EMRVKRRDAE QWMSHRLLPE NLRKRIRRYE QYKWQETRGV DEENLLSNLP KDLRRDIKRH LCLAL LMRV PMFEKMDEQL LDALCDRLQP VLYTEESYIV REGDPVDEML FIMRGKLLTI TTNGGRTGFL NSEYLGAGDF CGEELL TWA LDPHSSSNLP ISTRTVRALM EVEAFALKAD DLKFVASQFR RLHSKQLRHT FRYYSQQWKT WAACFIQAAW RRYIKKK LE ESLKEEENRL QDALAKEACG SSPSLGATIY ASRFAANILR TIRRSGSVRK PRMPERMPPM LLQKPAEPDF NSDD UniProtKB: Cyclic nucleotide-gated ion channel 1 |
-Macromolecule #2: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 3 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Macromolecule #3: water
Macromolecule | Name: water / type: ligand / ID: 3 / Number of copies: 8 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |