Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8J1E

AtSLAC1 in open state

Summary for 8J1E
Entry DOI10.2210/pdb8j1e/pdb
EMDB information35920
DescriptorGuard cell S-type anion channel SLAC1,Green fluorescent protein, CHOLESTEROL HEMISUCCINATE, CHLORIDE ION (3 entities in total)
Functional Keywordsstomatal closure, anion channel, phosphorylation-dependent activation, membrane protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains3
Total formula weight283261.76
Authors
Lee, Y.,Lee, S. (deposition date: 2023-04-12, release date: 2023-11-22, Last modification date: 2023-11-29)
Primary citationLee, Y.,Jeong, H.S.,Jung, S.,Hwang, J.,Le, C.T.H.,Jun, S.H.,Du, E.J.,Kang, K.,Kim, B.G.,Lim, H.H.,Lee, S.
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model.
Nat Commun, 14:7345-7345, 2023
Cited by
PubMed 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 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.
PubMed: 37963863
DOI: 10.1038/s41467-023-43193-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.84 Å)
Structure validation

238895

数据于2025-07-16公开中

PDB statisticsPDBj update infoContact PDBjnumon