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Yorodumi- EMDB-65146: Cryo-EM structure of SULTR-like phosphate distribution transporter -
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Basic information
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| Title | Cryo-EM structure of SULTR-like phosphate distribution transporter | |||||||||
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Keywords | Phosphate distribution transporter / SULTR-like / Homodimer / TRANSPORT PROTEIN | |||||||||
| Function / homology | Function and homology informationsecondary active sulfate transmembrane transporter activity / transmembrane transporter activity / transmembrane transport / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.67 Å | |||||||||
Authors | Liu Y / Zhang J / He H / Liu Z | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Sci China Life Sci / Year: 2026Title: Structural and dynamic insights into SPDT for phosphorus allocation in rice. Authors: Haitao He / Yan Liu / Jie Zhang / Xiaofeng Zheng / Lihuan Jiang / Zhangmeng Du / Jiaqi Zuo / Shuo Cao / Xuemei Peng / Zhiwen Zheng / Kun Li / Cuicui Shen / Yanke Chen / Ping Yin / Chuang ...Authors: Haitao He / Yan Liu / Jie Zhang / Xiaofeng Zheng / Lihuan Jiang / Zhangmeng Du / Jiaqi Zuo / Shuo Cao / Xuemei Peng / Zhiwen Zheng / Kun Li / Cuicui Shen / Yanke Chen / Ping Yin / Chuang Wang / Lizhong Xiong / Faming Dong / Zhu Liu / ![]() Abstract: Phosphorus is essential for plants, absorbed as inorganic phosphate (Pi) and distributed via specialized transporters. The SULTR-like phosphorus distribution transporter (SPDT) preferentially ...Phosphorus is essential for plants, absorbed as inorganic phosphate (Pi) and distributed via specialized transporters. The SULTR-like phosphorus distribution transporter (SPDT) preferentially allocates phosphorus to developing grains-an energetically costly process that can potentially be attenuated without affecting crop yield and germination, positioning SPDT as a prime target for sustainable agriculture. Here, we report cryo-EM structures of rice SPDT in Pi-bound and apo states, uncovering an elevator-type transport mechanism. The transmembrane region segregates into a mobile Pi-binding core domain and a stationary gate domain. Pi coordination involves specific residues within the core domain, followed by an electropositive vestibule that extends from the binding pocket to the cytoplasm. Integrative structural and smFRET analyses demonstrate a dynamic mechanism regulating the transporter's conformational equilibrium. In this mechanism, the transporter's intracellular STAS domain acts as a bidirectional conformation-switch: (i) membrane-proximal binding stabilizes the inward-facing state via interactions with the core/gate domains, while (ii) dissociation enables reset to the outward-facing state. This dynamic coupling elucidates the regulatory mechanism of the STAS domain, highlighting its universally conserved function across the SulP, SULTR, and SLC26 families. Our findings provide a mechanistic blueprint for engineering phosphorus allocation in crops to enhance nutrient-use efficiency. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_65146.map.gz | 230.1 MB | EMDB map data format | |
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| Header (meta data) | emd-65146-v30.xml emd-65146.xml | 19.3 KB 19.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_65146_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_65146.png | 61.4 KB | ||
| Filedesc metadata | emd-65146.cif.gz | 6.4 KB | ||
| Others | emd_65146_half_map_1.map.gz emd_65146_half_map_2.map.gz | 226.7 MB 226.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65146 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65146 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9vkyMC ![]() 9vl5C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_65146.map.gz / Format: CCP4 / Size: 244.1 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 | X=Y=Z: 0.73 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_65146_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_65146_half_map_2.map | ||||||||||||
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Sample components
-Entire : SULTR-like phosphate distribution transporter
| Entire | Name: SULTR-like phosphate distribution transporter |
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| Components |
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-Supramolecule #1: SULTR-like phosphate distribution transporter
| Supramolecule | Name: SULTR-like phosphate distribution transporter / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Os06g0143700 protein
| Macromolecule | Name: Os06g0143700 protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 72.05418 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MVVNNKVDSL SYDVEAPPAQ APTTPAVVSA PPTPRGEAPA MTTTAAAELH KVSVPERRST AKALRQRLAE VFFPDDPLHQ FKNQSSARR LVLALQYFFP IFHWGSDYSL RLLRSDVVSG LTIASLAIPQ GISYAKLANL PPIIGLYSSF VPPLIYSLLG S SRDLAVGP ...String: MVVNNKVDSL SYDVEAPPAQ APTTPAVVSA PPTPRGEAPA MTTTAAAELH KVSVPERRST AKALRQRLAE VFFPDDPLHQ FKNQSSARR LVLALQYFFP IFHWGSDYSL RLLRSDVVSG LTIASLAIPQ GISYAKLANL PPIIGLYSSF VPPLIYSLLG S SRDLAVGP VSIASLVMGS MLRQAVSPDQ EPILYLQLAF TSTFFAGVFQ ASLGFLRLGF IVDFLSKATL TGFMGGAAII VS LQQLKGL LGIIHFTSQM GFVQVMHSVF KHHDEWAWQT ILMGVAFLAV LLTTRHISAR NPKLFWVSAA APLTSVIIST IIS FVSKAH GISVIGDLPK GLNPPSANML TFSGSYVGLA LNTGIMTGIL SLTEGIAVGR TFASINNYQV DGNKEMMAIG VMNM AGSCA SCYVTTGSFS RSAVNYSAGC KTAVSNIVMA SAVLVTLLFL MPLFHYTPNV ILSAIIITAV IGLIDVRGAA RLWKV DKLD FLACMAAFLG VLLVSVQMGL AIAVGISLFK ILLQVTRPNM VVKGVVPGTA SYRSMAQYRE AMRVPSFLVV GVESAI YFA NSMYLGERIM RFLREEDERA AKCNQCPVRC IILDMSAVAA IDTSGLDALA ELKKVLEKRN IELVLANPVG SVTERLY NS VVGKTFGSDR VFFSVAEAVA AAPHKTQP UniProtKB: Os06g0143700 protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 Component:
Details: 150mM NaCl, 25mM Phosphate Buffer, 0.0001m/v LMNG, 0.000001m/v CHS | |||||||||||||||
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
China, 1 items
Citation



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Y (Row.)
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Homo sapiens (human)
Processing
FIELD EMISSION GUN

