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Yorodumi- PDB-9j2n: Cryo-EM structure of the human glucose transporter, GLUT7 in outw... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9j2n | |||||||||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of the human glucose transporter, GLUT7 in outward-facing open conformation | |||||||||||||||||||||||||||||||||||||||
Components | Solute carrier family 2, facilitated glucose transporter member 7 | |||||||||||||||||||||||||||||||||||||||
Keywords | TRANSPORT PROTEIN / Human glucose transporter 7 / SLC2A7 / Fructose transporter / Intestinal hexose absorption / Membrane protein | |||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationsugar transmembrane transporter activity / fructose transmembrane transporter activity / fructose transmembrane transport / dehydroascorbic acid transport / hexose transmembrane transport / Cellular hexose transport / D-glucose transmembrane transporter activity / D-glucose transmembrane transport / D-glucose import / apical plasma membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||||||||||||||||||||
Authors | Lee, S.S. / Kim, S. / Jin, M.S. | |||||||||||||||||||||||||||||||||||||||
| Funding support | Korea, Republic Of, 2items
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Citation | Journal: Biochem Biophys Res Commun / Year: 2024Title: Cryo-EM structure of the human glucose transporter GLUT7. Authors: Sang Soo Lee / Subin Kim / Mi Sun Jin / ![]() Abstract: GLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human ...GLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human GLUT7 in the apo state at 3.3 Å resolution. Our atomic model reveals a typical major facilitator superfamily fold, with the substrate-binding site open to the extracellular side of the membrane. Despite the nearly identical conformation to its closest family member, rat GLUT5, our structure unveils distinct features of the substrate-binding cavity that may influence substrate specificity and binding mode. A homology model of the inward-open human GLUT7 indicates that similar to other members of the GLUT family, it may undergo a global rocker-switch-like reorientation of the transmembrane bundles to facilitate substrate translocation across the membrane. Our work enhances the current structural understanding of the GLUT family, and lays a foundation for rational design of regulators of GLUTs and other sugar transporters. | |||||||||||||||||||||||||||||||||||||||
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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 | 9j2n.cif.gz | 91.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9j2n.ent.gz | 67.2 KB | Display | PDB format |
| PDBx/mmJSON format | 9j2n.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9j2n_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9j2n_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9j2n_validation.xml.gz | 32.5 KB | Display | |
| Data in CIF | 9j2n_validation.cif.gz | 45.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j2/9j2n ftp://data.pdbj.org/pub/pdb/validation_reports/j2/9j2n | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 61099MC 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: 55777.195 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SLC2A7, GLUT7 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q6PXP3 |
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| #2: Sugar | ChemComp-NAG / |
| Has ligand of interest | Y |
| Has protein modification | N |
-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
| Component | Name: human glucose transporter 7, SLC2A7 / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7 |
| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 20000 nm / Nominal defocus min: 4000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 112978 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
Korea, Republic Of, 2items
Citation
PDBj



Trichoplusia ni (cabbage looper)

FIELD EMISSION GUN