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- PDB-7w6k: Cryo-EM structure of GmALMT12/QUAC1 anion channel -

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Basic information

Entry
Database: PDB / ID: 7w6k
TitleCryo-EM structure of GmALMT12/QUAC1 anion channel
ComponentsGmALMT12/QUAC1
KeywordsMEMBRANE PROTEIN / Symmetrical dimer / T-shaped pore / twisted two-layer architecture / Malate-modulation
Function / homologymalate transport / Aluminum-activated malate transporter / Aluminium activated malate transporter / plant-type vacuole membrane / monoatomic ion transmembrane transport / membrane => GO:0016020 / Uncharacterized protein
Function and homology information
Biological speciesGlycine max (soybean)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsQin, L. / Tang, L.H. / Xu, J.S. / Zhang, X.H. / Zhu, Y. / Sun, F. / Su, M. / Zhai, Y.J. / Chen, Y.H.
Funding support China, 3items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2020YFA0509903, 2016YFA0500503, 2017YFA0504703 China
Chinese Academy of SciencesXDA24020305, XDB37040102, 153E11KYSB20190029 China
National Natural Science Foundation of China (NSFC)31872721, 31771566 China
CitationJournal: Sci Adv / Year: 2022
Title: Cryo-EM structure and electrophysiological characterization of ALMT from reveal a previously uncharacterized class of anion channels.
Authors: Li Qin / Ling-Hui Tang / Jia-Shu Xu / Xian-Hui Zhang / Yun Zhu / Chun-Rui Zhang / Mei-Hua Wang / Xue-Lei Liu / Fei Li / Fei Sun / Min Su / Yujia Zhai / Yu-Hang Chen /
Abstract: Aluminum-activated malate transporters (ALMTs) form an anion channel family that plays essential roles in diverse functions in plants. ALMT12, also named QUAC1 (quick anion channel 1), regulates ...Aluminum-activated malate transporters (ALMTs) form an anion channel family that plays essential roles in diverse functions in plants. ALMT12, also named QUAC1 (quick anion channel 1), regulates stomatal closure in response to environmental stimuli. However, the molecular basis of ALMT12/QUAC1 activity remains elusive. Here, we describe the cryo-EM structure of ALMT12/QUAC1 from at 3.5-Å resolution. ALMT12/QUAC1 is a symmetrical dimer, forming a single electropositive T-shaped pore across the membrane. The transmembrane and cytoplasmic domains are assembled into a twisted two-layer architecture, with their associated dimeric interfaces nearly perpendicular. ALMT12/QUAC1-mediated currents display rapid kinetics of activation/deactivation and a bell-shaped voltage dependency, reminiscent of the rapid (R)-type anion currents. Our structural and functional analyses reveal a domain-twisting mechanism for malate-mediated activation. Together, our study uncovers the molecular basis for a previously uncharacterized class of anion channels and provides insights into the gating and modulation of the ALMT12/QUAC1 anion channel.
History
DepositionDec 1, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 16, 2022Provider: repository / Type: Initial release

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Structure visualization

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Assembly

Deposited unit
A: GmALMT12/QUAC1
B: GmALMT12/QUAC1


Theoretical massNumber of molelcules
Total (without water)120,6442
Polymers120,6442
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: cross-linking
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area7810 Å2
ΔGint-84 kcal/mol
Surface area40730 Å2

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Components

#1: Protein GmALMT12/QUAC1


Mass: 60321.969 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Glycine max (soybean) / Gene: GLYMA_01G199400 / Production host: Schizosaccharomyces pombe (fission yeast) / References: UniProt: I1J9K0

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: GmALMT12/QUAC1 / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Glycine max (soybean)
Source (recombinant)Organism: Schizosaccharomyces pombe (fission yeast)
Buffer solutionpH: 8
SpecimenConc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 130000 X / Cs: 2.7 mm
Image recordingAverage exposure time: 8 sec. / Electron dose: 60 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 6189
Image scansMovie frames/image: 32

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Processing

EM software
IDNameVersionCategory
2cryoSPARC3.1particle selection
3SerialEM3.8image acquisition
5GctfCTF correction
11cryoSPARC3.1final Euler assignment
13cryoSPARC3.13D reconstruction
14PHENIXmodel refinement
CTF correctionType: NONE
Particle selectionNum. of particles selected: 2987283
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 169576 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL / Space: REAL

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