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- PDB-7en0: Structure and Activity of SLAC1 Channels for Stomatal Signaling i... -
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Basic information
Entry | Database: PDB / ID: 7en0 | ||||||||||||||||||
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Title | Structure and Activity of SLAC1 Channels for Stomatal Signaling in Leaves | ||||||||||||||||||
![]() | SLow Anion Channel 1 | ||||||||||||||||||
![]() | MEMBRANE PROTEIN / anion channel | ||||||||||||||||||
Function / homology | ![]() response to humidity / stomatal closure / regulation of stomatal opening / voltage-gated monoatomic anion channel activity / regulation of stomatal closure / response to ozone / intracellular monoatomic ion homeostasis / organic anion transport / response to carbon dioxide / response to abscisic acid ...response to humidity / stomatal closure / regulation of stomatal opening / voltage-gated monoatomic anion channel activity / regulation of stomatal closure / response to ozone / intracellular monoatomic ion homeostasis / organic anion transport / response to carbon dioxide / response to abscisic acid / multicellular organismal-level water homeostasis / response to light stimulus / protein phosphatase binding / membrane => GO:0016020 / protein kinase binding / plasma membrane Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.97 Å | ||||||||||||||||||
![]() | Deng, Y. / Kashtoh, H. / Wang, Q. / Zhen, G. / Li, Q. / Tang, L. / Gao, H. / Zhang, C. / Qin, L. / Su, M. ...Deng, Y. / Kashtoh, H. / Wang, Q. / Zhen, G. / Li, Q. / Tang, L. / Gao, H. / Zhang, C. / Qin, L. / Su, M. / Li, F. / Huang, X. / Wang, Y. / Xie, Q. / Clarke, O.B. / Hendrickson, W.A. / Chen, Y. | ||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure and activity of SLAC1 channels for stomatal signaling in leaves. Authors: Ya-Nan Deng / Hamdy Kashtoh / Quan Wang / Guang-Xiao Zhen / Qi-Yu Li / Ling-Hui Tang / Hai-Long Gao / Chun-Rui Zhang / Li Qin / Min Su / Fei Li / Xia-He Huang / Ying-Chun Wang / Qi Xie / ...Authors: Ya-Nan Deng / Hamdy Kashtoh / Quan Wang / Guang-Xiao Zhen / Qi-Yu Li / Ling-Hui Tang / Hai-Long Gao / Chun-Rui Zhang / Li Qin / Min Su / Fei Li / Xia-He Huang / Ying-Chun Wang / Qi Xie / Oliver B Clarke / Wayne A Hendrickson / Yu-Hang Chen / ![]() ![]() Abstract: Stomata in leaves regulate gas exchange between the plant and its atmosphere. Various environmental stimuli elicit abscisic acid (ABA); ABA leads to phosphoactivation of slow anion channel 1 (SLAC1); ...Stomata in leaves regulate gas exchange between the plant and its atmosphere. Various environmental stimuli elicit abscisic acid (ABA); ABA leads to phosphoactivation of slow anion channel 1 (SLAC1); SLAC1 activity reduces turgor pressure in aperture-defining guard cells; and stomatal closure ensues. We used electrophysiology for functional characterizations of SLAC1 (SLAC1) and cryoelectron microscopy (cryo-EM) for structural analysis of SLAC1 (SLAC1), at 2.97-Å resolution. We identified 14 phosphorylation sites in SLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated. Seven SLAC1-conserved arginines are poised in SLAC1 for regulatory interaction with the N-terminal extension. This SLAC1 structure has its pores closed, in a basal state, spring loaded by phenylalanyl residues in high-energy conformations. SLAC1 phosphorylation fine-tunes an equilibrium between basal and activated SLAC1 trimers, thereby controlling the degree of stomatal opening. | ||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 180.8 KB | Display | ![]() |
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PDB format | ![]() | 136.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 43.7 KB | Display | |
Data in CIF | ![]() | 57.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 31197MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 62678.348 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | Has ligand of interest | N | |
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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: Cryo-EM structure of Brachypodium distachyon SLAC1 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
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: UltrAuFoil R0.6/1 |
Vitrification | Cryogen name: ETHANE |
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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 |
Image recording | Electron dose: 71.3 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software | Name: cryoSPARC / Version: 2.0.27 / Category: 3D reconstruction |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C3 (3 fold cyclic) |
3D reconstruction | Resolution: 2.97 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 95704 / Symmetry type: POINT |