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Open data
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Basic information
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Title | Structure of the Medicago truncatula CNGC15b | |||||||||
![]() | 0.22 in chimera | |||||||||
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![]() | channel / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() arbuscular mycorrhizal association / nodulation / voltage-gated potassium channel activity / calcium channel activity / nuclear membrane / transmembrane transporter binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
![]() | Yang GH / Xu X / Yang JZ | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for the activity regulation of Medicago calcium channel CNGC15. Authors: Xia Xu / Qinrui Wang / Tengfei Sun / Heyi Gao / Ruichu Gu / Junzhao Yang / Jiaqi Zhou / Peng Fu / Han Wen / Guanghui Yang / ![]() Abstract: Cyclic nucleotide-gated ion channels (CNGCs) in plants mediate Ca influx in response to environmental changes. Among numerous plant CNGCs, Medicago truncatula CNGC15a/b/c (MtCNGC15) is localized to ...Cyclic nucleotide-gated ion channels (CNGCs) in plants mediate Ca influx in response to environmental changes. Among numerous plant CNGCs, Medicago truncatula CNGC15a/b/c (MtCNGC15) is localized to the nuclear envelope. The opening and closing cycle of MtCNGC15 is tightly associated with the Ca oscillation in symbiosis. However, the molecular mechanism underlying MtCNGC15 activity regulation remains unclear. In this study, we present the structures of MtCNGC15 in its apo form and in the presence of CaM. The apo MtCNGC15b exhibits a flexible cytoplasmic domain (CPD), whereas binding of the MtCaM inhibits Ca currents and stabilizes the highly dynamic CPD. Furthermore, the activity of MtCNGC15b seems to be independent of cGMP. The hypothetical binding pocket for cGMP is occupied by an arginine residue. These findings elucidate the structural basis for the activity regulation of nuclear localized MtCNGC15. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.1 KB 17.1 KB | Display Display | ![]() |
Images | ![]() | 59.6 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() ![]() | 31.6 MB 59.3 MB 59.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 820.1 KB | Display | ![]() |
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Full document | ![]() | 819.8 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 14.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9kcuMC ![]() 9kcvC 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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Annotation | 0.22 in chimera | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: 0.1 in chimera
File | emd_62261_additional_1.map | ||||||||||||
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Annotation | 0.1 in chimera | ||||||||||||
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Density Histograms |
-Half map: 0.128 in chimera
File | emd_62261_half_map_1.map | ||||||||||||
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Annotation | 0.128 in chimera | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: 0.128 in chimera
File | emd_62261_half_map_2.map | ||||||||||||
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Annotation | 0.128 in chimera | ||||||||||||
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Sample components
-Entire : homotetrameric channel
Entire | Name: homotetrameric channel |
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Components |
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-Supramolecule #1: homotetrameric channel
Supramolecule | Name: homotetrameric channel / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Protein CNGC15b
Macromolecule | Name: Protein CNGC15b / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 75.809562 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MVTPKFMSDL FEGDHLELAK LTSPNGDNGI KFNEKHVAPR VLSRVFSEDY KRVKRRRRIF DPRGQTIHQW NKIFLVACLI SLFVDPLFF YLPIVQDEVC IDIGIAVEVF LIIIRSIADV FYVIHIFMRF HTAYVAPSSR VFGRGELVID SSKIASRYLH K GFFLDFIA ...String: MVTPKFMSDL FEGDHLELAK LTSPNGDNGI KFNEKHVAPR VLSRVFSEDY KRVKRRRRIF DPRGQTIHQW NKIFLVACLI SLFVDPLFF YLPIVQDEVC IDIGIAVEVF LIIIRSIADV FYVIHIFMRF HTAYVAPSSR VFGRGELVID SSKIASRYLH K GFFLDFIA ALPLPQVLIW IVIPNLGGST IANTKNVLRF IIIIQYLPRL FLIFPLSSQI VKATGVVTET AWAGAAYNLI LY MLASHVL GACWYLLSIE RQEACWKSVC KLEESSCQFD FFDCNMVKDS LRVSWFVTSN VTNLCSPNSL FYQFGIYGDA VTS KVTTSA FFNKYFFCLW WGLRNLSSLG QGLLTSTFVG EIMFAIVIAT LGLVLFALLI GNMQTYLQST TVRLEEWRVK RTDT EQWMH HRQLPQELRQ SVRKYDQYKW IATRGVDEES LLRGLPLDLR RDIKRHLCLE LVRRVPLFDA MDERMLDAIC ERLKP ALCT ENTYLVREGD PVNEMLFIIR GNLDSYTTDG GRTGFFNSCR IGPGDFCGEE LLTWALDPRP TMVIPSSTRT VKAISE VEA FALIAEDLKF VASQFRRLHS KQLRNKLRFH SHQWRTWAAC FIQVAWRRTI QEKKGSCGSS AWSHPQFEKG GGSGGGS GG SAWSHPQFEK SGDYKDDDDK UniProtKB: Protein CNGC15b |
-Macromolecule #2: PHOSPHATIDYLETHANOLAMINE
Macromolecule | Name: PHOSPHATIDYLETHANOLAMINE / type: ligand / ID: 2 / Number of copies: 4 / Formula: PTY |
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Molecular weight | Theoretical: 734.039 Da |
Chemical component information | ![]() ChemComp-PTY: |
-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: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k 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: DIFFRACTION / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |