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

7VM8

Crystal structure of the MtDMI1 gating ring

Summary for 7VM8
Entry DOI10.2210/pdb7vm8/pdb
DescriptorIon channel DMI1 (1 entity in total)
Functional Keywordsdmi, symbiose, plant protein
Biological sourceMedicago truncatula (Barrel medic, Medicago tribuloides)
Total number of polymer chains1
Total formula weight60475.39
Authors
Huang, X.,Zhang, P. (deposition date: 2021-10-08, release date: 2022-08-24, Last modification date: 2023-11-29)
Primary citationLiu, H.,Lin, J.S.,Luo, Z.,Sun, J.,Huang, X.,Yang, Y.,Xu, J.,Wang, Y.F.,Zhang, P.,Oldroyd, G.E.D.,Xie, F.
Constitutive activation of a nuclear-localized calcium channel complex in Medicago truncatula.
Proc.Natl.Acad.Sci.USA, 119:e2205920119-e2205920119, 2022
Cited by
PubMed Abstract: Nuclear Ca oscillations allow symbiosis signaling, facilitating plant recognition of beneficial microsymbionts, nitrogen-fixing rhizobia, and nutrient-capturing arbuscular mycorrhizal fungi. Two classes of channels, DMI1 and CNGC15, in a complex on the nuclear membrane, coordinate symbiotic Ca oscillations. However, the mechanism of Ca signature generation is unknown. Here, we demonstrate spontaneous activation of this channel complex, through gain-of-function mutations in , leading to spontaneous nuclear Ca oscillations and spontaneous nodulation, in a -dependent manner. The mutations destabilize a hydrogen-bond or salt-bridge network between two RCK domains, with the resultant structural changes, alongside DMI1 cation permeability, activating the channel complex. This channel complex was reconstituted in human HEK293T cell lines, with the resultant calcium influx enhanced by autoactivated DMI1 and CNGC15s. Our results demonstrate the mode of activation of this nuclear channel complex, show that DMI1 and CNGC15 are sufficient to create oscillatory Ca signals, and provide insights into its native mode of induction.
PubMed: 35972963
DOI: 10.1073/pnas.2205920119
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.034 Å)
Structure validation

239492

数据于2025-07-30公开中

PDB statisticsPDBj update infoContact PDBjnumon