+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-34829 | |||||||||
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Title | AtALMT9 plus malate | |||||||||
Map data | ||||||||||
Sample |
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Keywords | CHANNEL / TRANSPORT PROTEIN | |||||||||
Function / homology | malate transport / Aluminum-activated malate transporter / Aluminium activated malate transporter / plant-type vacuole membrane / monoatomic anion channel activity / Aluminum-activated malate transporter 9 Function and homology information | |||||||||
Biological species | Arabidopsis thaliana (thale cress) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
Authors | Gong DS | |||||||||
Funding support | China, 1 items
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Citation | Journal: Cell Rep / Year: 2024 Title: Structural insight into the Arabidopsis vacuolar anion channel ALMT9 shows clade specificity. Authors: Dandan Qian / Yaru Chai / Weiping Li / Bin Cui / Shaoquan Lin / Zhibin Wang / Chongyuan Wang / Le Qing Qu / Deshun Gong / Abstract: The Arabidopsis thaliana aluminum-activated malate transporter 9 (AtALMT9) functions as a vacuolar chloride channel that regulates the stomatal aperture. Here, we present the cryoelectron microscopy ...The Arabidopsis thaliana aluminum-activated malate transporter 9 (AtALMT9) functions as a vacuolar chloride channel that regulates the stomatal aperture. Here, we present the cryoelectron microscopy (cryo-EM) structures of AtALMT9 in three distinct states. AtALMT9 forms a dimer, and the pore is lined with four positively charged rings. The apo-AtALMT9 state shows a putative endogenous citrate obstructing the pore, where two W120 constriction residues enclose a gate with a pore radius of approximately 1.8 Å, representing an open state. Interestingly, channel closure is solely controlled by W120. Compared to wild-type plants, the W120A mutant exhibits more sensitivity to drought stress and is unable to restore the visual phenotype on leaves upon water recovery, reflecting persistent stomatal opening. Furthermore, notable variations are noted in channel gating and substrate recognition of Glycine max ALMT12, AtALMT9, and AtALMT1. In summary, our investigation enhances comprehension of the interplay between structure and function within the ALMT family. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_34829.map.gz | 59.5 MB | EMDB map data format | |
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Header (meta data) | emd-34829-v30.xml emd-34829.xml | 13.2 KB 13.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_34829_fsc.xml | 8.5 KB | Display | FSC data file |
Images | emd_34829.png | 208.6 KB | ||
Filedesc metadata | emd-34829.cif.gz | 5.4 KB | ||
Others | emd_34829_half_map_1.map.gz emd_34829_half_map_2.map.gz | 59.2 MB 59.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-34829 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-34829 | HTTPS FTP |
-Validation report
Summary document | emd_34829_validation.pdf.gz | 787.8 KB | Display | EMDB validaton report |
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Full document | emd_34829_full_validation.pdf.gz | 787.4 KB | Display | |
Data in XML | emd_34829_validation.xml.gz | 16 KB | Display | |
Data in CIF | emd_34829_validation.cif.gz | 20.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34829 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34829 | HTTPS FTP |
-Related structure data
Related structure data | 8hiyMC 8hiwC 8zvfC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_34829.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size |
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Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_34829_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Dimer of AtALMT9
Entire | Name: Dimer of AtALMT9 |
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Components |
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-Supramolecule #1: Dimer of AtALMT9
Supramolecule | Name: Dimer of AtALMT9 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
-Macromolecule #1: Aluminum-activated malate transporter 9
Macromolecule | Name: Aluminum-activated malate transporter 9 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
Molecular weight | Theoretical: 67.121008 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MAAKQGSFRH GILEKRERLL SNNGFSDFRF TDIESNDLLE NENCGRRTRL CCCCSCGNLS EKISGVYDDA KDVARKAWEM GVSDPRKIV FSAKIGLALT IVALLIFYQE PNPDLSRYSV WAILTVVVVF EFTIGATLSK GFNRALGTLS AGGLALGMAE L STLFGDWE ...String: MAAKQGSFRH GILEKRERLL SNNGFSDFRF TDIESNDLLE NENCGRRTRL CCCCSCGNLS EKISGVYDDA KDVARKAWEM GVSDPRKIV FSAKIGLALT IVALLIFYQE PNPDLSRYSV WAILTVVVVF EFTIGATLSK GFNRALGTLS AGGLALGMAE L STLFGDWE EIFCTLSIFC IGFLATFMKL YPSMKAYEYG FRVFLLTYCY ILISGFRTGQ FIEVAISRFL LIALGAGVSL GV NMFIYPI WAGEDLHNLV VKNFMNVATS LEGCVNGYLR CLEYERIPSK ILTYQASEDP VYKGYRSAVE STSQEESLMS FAI WEPPHG PYKSFNYPWK NYVKLSGALK HCAFTVMALH GCILSEIQAP EERRQVFRQE LQRVGVEGAK LLRELGEKVK KMEK LGPVD LLFEVHLAAE ELQHKIDKKS YLLVNSECWE IGNRATKESE PQELLSLEDS DPPENHAPPI YAFKSLSEAV LEIPP SWGE KNHREALNHR PTFSKQVSWP ARLVLPPHLE TTNGASPLVE TTKTYESASA LSLATFASLL IEFVARLQNV VDAFKE LSQ KANFKEPEIV TTGTDVEFSG ERVGLGQKIR RCFGM UniProtKB: Aluminum-activated malate transporter 9 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |