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- PDB-6rtc: Structure of murine Solute Carrier 26 family member A9 (Slc26a9) ... -

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Basic information

Entry
Database: PDB / ID: 6rtc
TitleStructure of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in the inward-facing state
ComponentsSolute carrier family 26 member 9,Solute carrier family 26 member 9
KeywordsMEMBRANE PROTEIN / SLC26 family / anion transporter / membrane protein structure / transport mechanism / cryo-EM / single particle
Function / homology
Function and homology information


Multifunctional anion exchangers / oxalate transmembrane transporter activity / sulfate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / solute:inorganic anion antiporter activity / regulation of pH / bicarbonate transmembrane transporter activity / bicarbonate transport / monoatomic anion transport / chloride transport ...Multifunctional anion exchangers / oxalate transmembrane transporter activity / sulfate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / solute:inorganic anion antiporter activity / regulation of pH / bicarbonate transmembrane transporter activity / bicarbonate transport / monoatomic anion transport / chloride transport / chloride transmembrane transporter activity / chloride channel activity / chloride transmembrane transport / ATPase binding / apical plasma membrane / positive regulation of gene expression / cell surface / identical protein binding / plasma membrane
Similarity search - Function
Solute carrier family 26 member 9 / SLC26A/SulP transporter / SLC26A/SulP transporter domain / Sulfate permease family / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily
Similarity search - Domain/homology
Solute carrier family 26 member 9 / Solute carrier family 26 member 9
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.96 Å
AuthorsSawicka, M. / Walter, J.D. / Dutzler, R.
Funding support1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_163421
CitationJournal: 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
DepositionMay 23, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 24, 2019Provider: repository / Type: Initial release
Revision 1.1Aug 7, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Dec 18, 2019Group: Other / Category: atom_sites / cell
Item: _atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][2] ..._atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][2] / _atom_sites.fract_transf_matrix[3][3] / _cell.Z_PDB

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Structure visualization

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Assembly

Deposited unit
A: Solute carrier family 26 member 9,Solute carrier family 26 member 9
B: Solute carrier family 26 member 9,Solute carrier family 26 member 9


Theoretical massNumber of molelcules
Total (without water)141,1952
Polymers141,1952
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area8410 Å2
ΔGint-46 kcal/mol
Surface area57440 Å2
MethodPISA

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Components

#1: Protein Solute carrier family 26 member 9,Solute carrier family 26 member 9 / Anion transporter/exchanger protein 9


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

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Homodimer of Solute Carrier 26 family member A9 (Slc26a9)
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: homo sapiens (human)
Buffer solutionpH: 7.4
Buffer component
IDConc.NameFormulaBuffer-ID
110 mMHEPESC8H18N2O4S1
2200 mMsodium chlorideNaClSodium chloride1
30.02 %glycol-diosgeninC56H92O251
SpecimenConc.: 3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 46511 X / Calibrated magnification: 46511 X
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 0.2 sec. / Electron dose: 70 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 2838
Image scansMovie frames/image: 65

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Processing

SoftwareName: PHENIX / Version: 1.15.2_3472: / Classification: refinement
EM software
IDNameVersionCategory
2SerialEM3.5image acquisition
4CTFFIND4.1CTF correction
10RELION3initial Euler assignment
11RELION3final Euler assignment
13RELION33D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 416164
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.96 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 112930 / Symmetry type: POINT

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