+Open data
-Basic information
Entry | Database: PDB / ID: 8j0j | |||||||||||||||
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Title | AtSLAC1 8D mutant in closed state | |||||||||||||||
Components | Guard cell S-type anion channel SLAC1,Green fluorescent protein | |||||||||||||||
Keywords | MEMBRANE PROTEIN / Stomatal closure / anion channel / phosphorylation-dependent activation | |||||||||||||||
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 / monoatomic anion transmembrane transporter activity / response to abscisic acid / response to carbon dioxide / multicellular organismal-level water homeostasis / monoatomic anion transport / abscisic acid-activated signaling pathway / response to light stimulus / bioluminescence / generation of precursor metabolites and energy / protein phosphatase binding / protein kinase binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Arabidopsis thaliana (thale cress) Aequorea victoria (jellyfish) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||||||||
Authors | Lee, Y. / Lee, S. | |||||||||||||||
Funding support | Korea, Republic Of, 4items
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Citation | Journal: Nat Commun / Year: 2023 Title: Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model. Authors: Yeongmok Lee / Hyeon Seong Jeong / Seoyeon Jung / Junmo Hwang / Chi Truc Han Le / Sung-Hoon Jun / Eun Jo Du / KyeongJin Kang / Beom-Gi Kim / Hyun-Ho Lim / Sangho Lee / Abstract: The anion channel SLAC1 functions as a crucial effector in the ABA signaling, leading to stomata closure. SLAC1 is activated by phosphorylation in its intracellular domains. Both a binding-activation ...The anion channel SLAC1 functions as a crucial effector in the ABA signaling, leading to stomata closure. SLAC1 is activated by phosphorylation in its intracellular domains. Both a binding-activation model and an inhibition-release model for activation have been proposed based on only the closed structures of SLAC1, rendering the structure-based activation mechanism controversial. Here we report cryo-EM structures of Arabidopsis SLAC1 WT and its phosphomimetic mutants in open and closed states. Comparison of the open structure with the closed ones reveals the structural basis for opening of the conductance pore. Multiple phosphorylation of an intracellular domain (ICD) causes dissociation of ICD from the transmembrane domain. A conserved, positively-charged sequence motif in the intracellular loop 2 (ICL2) seems to be capable of sensing of the negatively charged phosphorylated ICD. Interactions between ICL2 and ICD drive drastic conformational changes, thereby widening the pore. From our results we propose that SLAC1 operates by a mechanism combining the binding-activation and inhibition-release models. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8j0j.cif.gz | 260.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8j0j.ent.gz | 190.2 KB | Display | PDB format |
PDBx/mmJSON format | 8j0j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j0/8j0j ftp://data.pdbj.org/pub/pdb/validation_reports/j0/8j0j | HTTPS FTP |
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-Related structure data
Related structure data | 35904MC 8gw6C 8gw7C 8j1eC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: ens_1
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