+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32633 | |||||||||||||||||||||
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Title | Cryo-EM structure of AtSLAC1 S59A mutant | |||||||||||||||||||||
Map data | Cryo-EM map of the AtSLAC1 S59A mutant | |||||||||||||||||||||
Sample |
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Keywords | anion channel / SLAC1 / stomata / guard cell / TRANSPORT PROTEIN | |||||||||||||||||||||
Function / homology | Function and homology information response to humidity / stomatal closure / regulation of stomatal opening / inorganic anion transport / voltage-gated monoatomic anion channel activity / regulation of stomatal closure / stomatal movement / response to ozone / intracellular monoatomic ion homeostasis / organic anion transport ...response to humidity / stomatal closure / regulation of stomatal opening / inorganic anion transport / voltage-gated monoatomic anion channel activity / regulation of stomatal closure / stomatal movement / response to ozone / intracellular monoatomic ion homeostasis / organic anion transport / response to carbon dioxide / monoatomic anion transmembrane transporter activity / response to abscisic acid / multicellular organismal-level water homeostasis / monoatomic anion transport / abscisic acid-activated signaling pathway / response to light stimulus / protein phosphatase binding / protein kinase binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | Arabidopsis thaliana (thale cress) | |||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||||||||||||||
Authors | Sun L / Liu X | |||||||||||||||||||||
Funding support | China, 6 items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation. Authors: Yawen Li / Yinan Ding / Lili Qu / Xinru Li / Qinxuan Lai / Pingxia Zhao / Yongxiang Gao / Chengbin Xiang / Chunlei Cang / Xin Liu / Linfeng Sun / Abstract: Stomata play a critical role in the regulation of gas exchange and photosynthesis in plants. Stomatal closure participates in multiple stress responses, and is regulated by a complex network ...Stomata play a critical role in the regulation of gas exchange and photosynthesis in plants. Stomatal closure participates in multiple stress responses, and is regulated by a complex network including abscisic acid (ABA) signaling and ion-flux-induced turgor changes. The slow-type anion channel SLAC1 has been identified to be a central controller of stomatal closure and phosphoactivated by several kinases. Here, we report the structure of SLAC1 in Arabidopsis thaliana (AtSLAC1) in an inactivated, closed state. The cytosolic amino (N)-terminus and carboxyl (C)-terminus of AtSLAC1 are partially resolved and form a plug-like structure which packs against the transmembrane domain (TMD). Breaking the interactions between the cytosolic plug and transmembrane domain triggers channel activation. An inhibition-release model is proposed for SLAC1 activation by phosphorylation that the cytosolic plug dissociates from the transmembrane domain upon phosphorylation, and induces conformational changes to open the pore. These findings facilitate our understanding of the regulation of SLAC1 activity and stomatal aperture in plants. | |||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32633.map.gz | 59.8 MB | EMDB map data format | |
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Header (meta data) | emd-32633-v30.xml emd-32633.xml | 16 KB 16 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_32633_fsc.xml | 9.1 KB | Display | FSC data file |
Images | emd_32633.png | 106.3 KB | ||
Filedesc metadata | emd-32633.cif.gz | 5.7 KB | ||
Others | emd_32633_half_map_1.map.gz emd_32633_half_map_2.map.gz | 59 MB 59 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32633 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32633 | HTTPS FTP |
-Validation report
Summary document | emd_32633_validation.pdf.gz | 763.5 KB | Display | EMDB validaton report |
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Full document | emd_32633_full_validation.pdf.gz | 763.1 KB | Display | |
Data in XML | emd_32633_validation.xml.gz | 16.4 KB | Display | |
Data in CIF | emd_32633_validation.cif.gz | 21.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32633 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32633 | HTTPS FTP |
-Related structure data
Related structure data | 7wnqMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_32633.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Cryo-EM map of the AtSLAC1 S59A mutant | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: half map 2
File | emd_32633_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 1
File | emd_32633_half_map_2.map | ||||||||||||
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Annotation | half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Trimeric structure of the anion channel SLAC1
Entire | Name: Trimeric structure of the anion channel SLAC1 |
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Components |
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-Supramolecule #1: Trimeric structure of the anion channel SLAC1
Supramolecule | Name: Trimeric structure of the anion channel SLAC1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
-Macromolecule #1: Guard cell S-type anion channel SLAC1
Macromolecule | Name: Guard cell S-type anion channel SLAC1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
Molecular weight | Theoretical: 63.311742 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MERKQSNAHS TFADINEVED EAEQELQQQE NNNNKRFSGN RGPNRGKQRP FRGFSRQVSL ETGFSVLNRE SRERDDKKSL PRSGRSFGG FESGGIINGG DGRKTDFSMF RTKSTLSKQK SLLPSIIRER DIENSLRTED GETKDDSINE NVSAGRYFAA L RGPELDEV ...String: MERKQSNAHS TFADINEVED EAEQELQQQE NNNNKRFSGN RGPNRGKQRP FRGFSRQVSL ETGFSVLNRE SRERDDKKSL PRSGRSFGG FESGGIINGG DGRKTDFSMF RTKSTLSKQK SLLPSIIRER DIENSLRTED GETKDDSINE NVSAGRYFAA L RGPELDEV KDNEDILLPK EEQWPFLLRF PIGCFGICLG LSSQAVLWLA LAKSPATNFL HITPLINLVV WLFSLVVLVS VS FTYILKC IFYFEAVKRE YFHPVRVNFF FAPWVVCMFL AISVPPMFSP NRKYLHPAIW CVFMGPYFFL ELKIYGQWLS GGK RRLCKV ANPSSHLSVV GNFVGAILAS KVGWDEVAKF LWAVGFAHYL VVFVTLYQRL PTSEALPKEL HPVYSMFIAA PSAA SIAWN TIYGQFDGCS RTCFFIALFL YISLVARINF FTGFKFSVAW WSYTFPMTTA SVATIKYAEA VPGYPSRALA LTLSF ISTA MVCVLFVSTL LHAFVWQTLF PNDLAIAITK RKLTREKKPF KRAYDLKRWT KQALAKKISA EKDFEAEEES HH UniProtKB: Guard cell S-type anion channel SLAC1 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281.0 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |