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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | IAA-bound AUX1 | |||||||||
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Keywords | transport / LeuT-fold / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationroot hair cell differentiation / auxin binding / root cap development / lateral root formation / auxin influx transmembrane transporter activity / positive gravitropism / establishment of planar polarity / auxin polar transport / auxin-activated signaling pathway / symporter activity ...root hair cell differentiation / auxin binding / root cap development / lateral root formation / auxin influx transmembrane transporter activity / positive gravitropism / establishment of planar polarity / auxin polar transport / auxin-activated signaling pathway / symporter activity / amino acid transmembrane transporter activity / response to nematode / endosome / cell surface / Golgi apparatus / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.52 Å | |||||||||
Authors | Wang CC / Jing D / Kong F / Huang GXY / Shi YG | |||||||||
| Funding support | 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2025Title: Structural basis of auxin binding and transport by AUX1. Authors: Dan Jing / Fang Kong / Xiaoli Lu / Gaoxingyu Huang / Jing Huang / Haolin Wang / Yigong Shi / Chengcheng Wang / ![]() Abstract: Indole-3-acetic acid (IAA), the major form of auxin, is essential for plant growth. Auxin resistant 1 (AUX1), the first identified auxin importer, plays a crucial role in polar auxin transport (PAT). ...Indole-3-acetic acid (IAA), the major form of auxin, is essential for plant growth. Auxin resistant 1 (AUX1), the first identified auxin importer, plays a crucial role in polar auxin transport (PAT). Here, we present cryo-EM structures of AUX1 in the IAA-free and IAA-bound states. AUX1 exists as a monomer that contains 11 transmembrane helices (TMs). TMs 1 to 5 and 6 to 10 constitute the two halves of a classic LeuT-fold, and TM11 interacts with both halves at the interface. In the IAA-bound state, IAA is specifically recognized in a central pocket formed by TM1, TM3, TM6, and TM8. In the presence of IAA, TM1 and TM6 undergo marked conformational changes that are critical for IAA transport. His249 stands out to be a key residue for substrate uptake and release. Our structures reveal the molecular basis for AUX1-mediated IAA binding and transport. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_63417.map.gz | 25.4 MB | EMDB map data format | |
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| Header (meta data) | emd-63417-v30.xml emd-63417.xml | 17.3 KB 17.3 KB | Display Display | EMDB header |
| Images | emd_63417.png | 86.3 KB | ||
| Masks | emd_63417_msk_1.map | 27 MB | Mask map | |
| Filedesc metadata | emd-63417.cif.gz | 6 KB | ||
| Others | emd_63417_half_map_1.map.gz emd_63417_half_map_2.map.gz | 25.1 MB 25.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63417 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63417 | HTTPS FTP |
-Validation report
| Summary document | emd_63417_validation.pdf.gz | 726.5 KB | Display | EMDB validaton report |
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| Full document | emd_63417_full_validation.pdf.gz | 726.1 KB | Display | |
| Data in XML | emd_63417_validation.xml.gz | 10.2 KB | Display | |
| Data in CIF | emd_63417_validation.cif.gz | 12 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63417 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63417 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9lvaMC ![]() 9lvbC 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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Map
| File | Download / File: emd_63417.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Voxel size | X=Y=Z: 1.0773 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_63417_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_63417_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_63417_half_map_2.map | ||||||||||||
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Sample components
-Entire : AUX1
| Entire | Name: AUX1 |
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| Components |
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-Supramolecule #1: AUX1
| Supramolecule | Name: AUX1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Auxin transporter protein 1
| Macromolecule | Name: Auxin transporter protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 57.131629 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MHHHHHHHHH HGSVEDYKDD DDKGSMSEGV EAIVANDNGT DQVNGNRTGK DNEEHDGSTG SNLSNFLWHG GSVWDAWFSC ASNQVAQVL LTLPYSFSQL GMLSGIVLQI FYGLLGSWTA YLISVLYVEY RARKEKEGKS FKNHVIQWFE VLDGLLGSYW K ALGLAFNC ...String: MHHHHHHHHH HGSVEDYKDD DDKGSMSEGV EAIVANDNGT DQVNGNRTGK DNEEHDGSTG SNLSNFLWHG GSVWDAWFSC ASNQVAQVL LTLPYSFSQL GMLSGIVLQI FYGLLGSWTA YLISVLYVEY RARKEKEGKS FKNHVIQWFE VLDGLLGSYW K ALGLAFNC TFLLFGSVIQ LIACASNIYY INDHLDKRTW TYIFGACCAT TVFIPSFHNY RIWSFLGLGM TTYTAWYLAI AS IIHGQAE GVKHSGPTKL VLYFTGATNI LYTFGGHAVT VEIMHAMWKP QKFKYIYLMA TLYVFTLTIP SAAAVYWAFG DAL LDHSNA FSLMPKNAWR DAAVILMLIH QFITFGFACT PLYFVWEKVI GMHDTKSICL RALARLPVVI PIWFLAIIFP FFGP INSAV GALLVSFTVY IIPSLAHMLT YRSASARQNA AEKPPFFMPS WTAMYVLNAF VVVWVLIVGF GFGGWASVTN FVRQV DTFG LFAKCYQCKP AAAAAHAPVS ALHHRL UniProtKB: Auxin transporter protein 1 |
-Macromolecule #2: 1H-INDOL-3-YLACETIC ACID
| Macromolecule | Name: 1H-INDOL-3-YLACETIC ACID / type: ligand / ID: 2 / Number of copies: 1 / Formula: IAC |
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| Molecular weight | Theoretical: 175.184 Da |
| Chemical component information | ![]() ChemComp-IAC: |
-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 |
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| Sugar embedding | Material: LMNG/CHS |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k 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: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Homo sapiens (human)
Processing
FIELD EMISSION GUN
