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Open data
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Basic information
Entry | Database: PDB / ID: 7wnq | |||||||||||||||||||||
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Title | Cryo-EM structure of AtSLAC1 S59A mutant | |||||||||||||||||||||
![]() | Guard cell S-type anion channel SLAC1 | |||||||||||||||||||||
![]() | TRANSPORT PROTEIN / anion channel / SLAC1 / stomata / guard cell | |||||||||||||||||||||
Function / homology | ![]() 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 | ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||||||||||||||
Model details | cryo-EM analysis of the plant S-type anion chennel | |||||||||||||||||||||
![]() | Sun, L. / Liu, X. / Li, Y. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() 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
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 203.5 KB | Display | ![]() |
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PDB format | ![]() | 161.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 41.8 KB | Display | |
Data in CIF | ![]() | 63.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 32633MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 63311.742 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SLAC1, CDI3, OZS1, RCD3, At1g12480, F5O11.23, T12C24.3 Plasmid: pCAG / Cell line (production host): HEK293F / Production host: ![]() |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Trimeric structure of the anion channel SLAC1 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
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Processing
EM software | Name: cryoSPARC / Version: 3.2.0 / Category: 3D reconstruction |
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CTF correction | Type: NONE |
Symmetry | Point symmetry: C3 (3 fold cyclic) |
3D reconstruction | Resolution: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 264751 / Symmetry type: POINT |