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Yorodumi- PDB-6rtf: Structure of murine Solute Carrier 26 family member A9 (Slc26a9) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6rtf | ||||||
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Title | Structure of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in an intermediate state | ||||||
Components | Solute carrier family 26 member 9,Solute carrier family 26 member 9 | ||||||
Keywords | MEMBRANE PROTEIN / SLC26 family / anion transporter / membrane protein structure / transport mechanism / cryo-EM / single particle | ||||||
Function / homology | Function and homology information Multifunctional anion exchangers / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / regulation of pH / solute:inorganic anion antiporter activity / bicarbonate transport / bicarbonate transmembrane transporter activity / monoatomic anion transport / chloride transport / chloride transmembrane transporter activity ...Multifunctional anion exchangers / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / regulation of pH / solute:inorganic anion antiporter activity / bicarbonate transport / bicarbonate transmembrane transporter activity / monoatomic anion transport / chloride transport / chloride transmembrane transporter activity / chloride channel activity / chloride transmembrane transport / ATPase binding / endosome membrane / apical plasma membrane / Golgi membrane / positive regulation of gene expression / endoplasmic reticulum membrane / cell surface / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.77 Å | ||||||
Authors | Sawicka, M. / Walter, J.D. / Dutzler, R. | ||||||
Funding support | 1items
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Citation | Journal: Elife / Year: 2019 Title: Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport. Authors: Justin D Walter / Marta Sawicka / Raimund Dutzler / Abstract: The epithelial anion transporter SLC26A9 contributes to airway surface hydration and gastric acid production. Colocalizing with CFTR, SLC26A9 has been proposed as a target for the treatment of cystic ...The epithelial anion transporter SLC26A9 contributes to airway surface hydration and gastric acid production. Colocalizing with CFTR, SLC26A9 has been proposed as a target for the treatment of cystic fibrosis. To provide molecular details of its transport mechanism, we present cryo-EM structures and a functional characterization of murine Slc26a9. These structures define the general architecture of eukaryotic SLC26 family members and reveal an unusual mode of oligomerization which relies predominantly on the cytosolic STAS domain. Our data illustrates conformational transitions of Slc26a9, supporting a rapid alternate-access mechanism which mediates uncoupled chloride transport with negligible bicarbonate or sulfate permeability. The characterization of structure-guided mutants illuminates the properties of the ion transport path, including a selective anion binding site located in the center of a mobile module within the transmembrane domain. This study thus provides a structural foundation for the understanding of the entire SLC26 family and potentially facilitates their therapeutic exploitation. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6rtf.cif.gz | 175.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6rtf.ent.gz | 122.3 KB | Display | PDB format |
PDBx/mmJSON format | 6rtf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6rtf_validation.pdf.gz | 975.7 KB | Display | wwPDB validaton report |
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Full document | 6rtf_full_validation.pdf.gz | 975.3 KB | Display | |
Data in XML | 6rtf_validation.xml.gz | 37.4 KB | Display | |
Data in CIF | 6rtf_validation.cif.gz | 58.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rt/6rtf ftp://data.pdbj.org/pub/pdb/validation_reports/rt/6rtf | HTTPS FTP |
-Related structure data
Related structure data | 4998MC 4997C 6rtcC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 70597.641 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Slc26a9, mCG_51751 / Cell line (production host): HEK293S GnTI- / Production host: Homo sapiens (human) / References: UniProt: A0A0R4J0F7, UniProt: Q8BU91*PLUS |
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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 |
-Sample preparation
Component | Name: Murine Solute Carrier 26 family member A9 (Slc26a9) in MSP1E3D1 nanodisc Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Mus musculus (house mouse) |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.4 |
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % |
-Electron microscopy imaging
Experimental equipment | Model: Tecnai Polara / Image courtesy: FEI Company |
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Microscopy | Model: FEI POLARA 300 |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 37313 X / Calibrated magnification: 37313 X |
Specimen holder | Cryogen: NITROGEN |
Image recording | Average exposure time: 0.25 sec. / Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 3134 |
Image scans | Movie frames/image: 50 |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 711032 | ||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 7.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17442 / Symmetry type: POINT |