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Yorodumi- PDB-7y9u: Structure of the auxin exporter PIN1 in Arabidopsis thaliana in t... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7y9u | |||||||||||||||
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| Title | Structure of the auxin exporter PIN1 in Arabidopsis thaliana in the NPA-bound state | |||||||||||||||
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Keywords | TRANSPORT PROTEIN | |||||||||||||||
| Function / homology | Function and homology informationcotyledon morphogenesis / leaf formation / cotyledon development / leaf shaping / shoot system development / xylem and phloem pattern formation / inflorescence development / gravitropism / auxin export across the plasma membrane / auxin efflux transmembrane transporter activity ...cotyledon morphogenesis / leaf formation / cotyledon development / leaf shaping / shoot system development / xylem and phloem pattern formation / inflorescence development / gravitropism / auxin export across the plasma membrane / auxin efflux transmembrane transporter activity / flower development / auxin polar transport / root development / plant-type cell wall / photomorphogenesis / embryo development ending in seed dormancy / auxin-activated signaling pathway / plasmodesma / basal plasma membrane / cell periphery / apical part of cell / apical plasma membrane / protein homodimerization activity / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | ![]() ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||
Authors | Sun, L. / Liu, X. / Yang, Z. / Xia, J. | |||||||||||||||
| Funding support | China, 4items
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Citation | Journal: Nature / Year: 2022Title: Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Authors: Zhisen Yang / Jing Xia / Jingjing Hong / Chenxi Zhang / Hong Wei / Wei Ying / Chunqiao Sun / Lianghanxiao Sun / Yanbo Mao / Yongxiang Gao / Shutang Tan / Jiří Friml / Dianfan Li / Xin Liu / Linfeng Sun / ![]() Abstract: Polar auxin transport is unique to plants and coordinates their growth and development. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and ...Polar auxin transport is unique to plants and coordinates their growth and development. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport; however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of Arabidopsis thaliana PIN1: the apo state, bound to the natural auxin indole-3-acetic acid (IAA), and in complex with the polar auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of PIN1 shares a conserved NhaA fold. In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site at the intracellular pocket, but with a much higher affinity. These findings inform our understanding of the substrate recognition and transport mechanisms of PINs and set up a framework for future research on directional auxin transport, one of the most crucial processes underlying plant development. | |||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7y9u.cif.gz | 186.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7y9u.ent.gz | 143.6 KB | Display | PDB format |
| PDBx/mmJSON format | 7y9u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7y9u_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 7y9u_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 7y9u_validation.xml.gz | 40.9 KB | Display | |
| Data in CIF | 7y9u_validation.cif.gz | 61.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y9/7y9u ftp://data.pdbj.org/pub/pdb/validation_reports/y9/7y9u | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 33692MC ![]() 7y9tC ![]() 7y9vC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 67080.781 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human) / References: UniProt: Q9C6B8#2: Antibody | Mass: 13369.910 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | Has ligand of interest | Y | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
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| Source (recombinant) |
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| Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: DIFFRACTION / Nominal defocus max: 2300 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 215094 / Symmetry type: POINT |
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China, 4items
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gel filtration
Homo sapiens (human)

