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Yorodumi- EMDB-17085: Structure of Human Solute Carrier 26 family member A6 (SLC26A6) a... -
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Basic information
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| Title | Structure of Human Solute Carrier 26 family member A6 (SLC26A6) anion transporter in an inward-facing state | |||||||||
Map data | Final cryo-EM density map of human SLC26A6 | |||||||||
Sample |
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Keywords | Homodimer / Transporter / Exchanger / Bicarbonate / Chloride / Oxalate MEMBRANE PROTEIN / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationsulfate:bicarbonate antiporter activity / mannitol transmembrane transport / formate transport / oxalate transport / oxalic acid secretion / formate transmembrane transporter activity / protein kinase C signaling / Inorganic anion exchange by SLC26 transporters / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity ...sulfate:bicarbonate antiporter activity / mannitol transmembrane transport / formate transport / oxalate transport / oxalic acid secretion / formate transmembrane transporter activity / protein kinase C signaling / Inorganic anion exchange by SLC26 transporters / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / transepithelial chloride transport / epithelial fluid transport / sulfate transmembrane transport / secondary active sulfate transmembrane transporter activity / intracellular pH elevation / cellular response to fructose stimulus / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / transepithelial transport / bicarbonate transport / bicarbonate transmembrane transporter activity / vesicle membrane / chloride transport / chloride transmembrane transporter activity / intestinal absorption / sperm capacitation / chloride channel activity / efflux transmembrane transporter activity / chloride channel complex / estrous cycle / monoatomic ion transport / sperm midpiece / positive regulation of dipeptide transmembrane transport / cytoplasmic vesicle membrane / chloride transmembrane transport / cellular response to cAMP / angiotensin-activated signaling pathway / regulation of intracellular pH / PDZ domain binding / establishment of localization in cell / brush border membrane / cellular response to type II interferon / transferase activity / basolateral plasma membrane / vesicle / apical plasma membrane / endoplasmic reticulum / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.28 Å | |||||||||
Authors | Tippett DN / Breen C / Butler SJ / Sawicka M / Dutzler R | |||||||||
| Funding support | Switzerland, 1 items
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Citation | Journal: Elife / Year: 2023Title: Structural and functional properties of the transporter SLC26A6 reveal mechanism of coupled anion exchange. Authors: David N Tippett / Colum Breen / Stephen J Butler / Marta Sawicka / Raimund Dutzler / ![]() Abstract: Members of the SLC26 family constitute a conserved class of anion transport proteins, which encompasses uncoupled transporters with channel-like properties, coupled exchangers and motor proteins. ...Members of the SLC26 family constitute a conserved class of anion transport proteins, which encompasses uncoupled transporters with channel-like properties, coupled exchangers and motor proteins. Among the 10 functional paralogs in humans, several participate in the secretion of bicarbonate in exchange with chloride and thus play an important role in maintaining pH homeostasis. Previously, we have elucidated the structure of murine SLC26A9 and defined its function as an uncoupled chloride transporter (Walter et al., 2019). Here we have determined the structure of the closely related human transporter SLC26A6 and characterized it as a coupled exchanger of chloride with bicarbonate and presumably also oxalate. The structure defines an inward-facing conformation of the protein that generally resembles known structures of SLC26A9. The altered anion selectivity between both paralogs is a consequence of a remodeled ion binding site located in the center of a mobile unit of the membrane-inserted domain, which also accounts for differences in the coupling mechanism. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_17085.map.gz | 277.6 MB | EMDB map data format | |
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| Header (meta data) | emd-17085-v30.xml emd-17085.xml | 16.6 KB 16.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_17085_fsc.xml | 14.3 KB | Display | FSC data file |
| Images | emd_17085.png | 122.3 KB | ||
| Masks | emd_17085_msk_1.map | 307.5 MB | Mask map | |
| Filedesc metadata | emd-17085.cif.gz | 6.1 KB | ||
| Others | emd_17085_half_map_1.map.gz emd_17085_half_map_2.map.gz | 284.8 MB 284.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17085 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17085 | HTTPS FTP |
-Validation report
| Summary document | emd_17085_validation.pdf.gz | 966.2 KB | Display | EMDB validaton report |
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| Full document | emd_17085_full_validation.pdf.gz | 965.8 KB | Display | |
| Data in XML | emd_17085_validation.xml.gz | 23.4 KB | Display | |
| Data in CIF | emd_17085_validation.cif.gz | 30.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17085 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17085 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8opqMC 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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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_17085.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Final cryo-EM density map of human SLC26A6 | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.651 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_17085_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: Half-map 2 of human SLC26A6
| File | emd_17085_half_map_1.map | ||||||||||||
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| Annotation | Half-map 2 of human SLC26A6 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half-map 1 of human SLC26A6
| File | emd_17085_half_map_2.map | ||||||||||||
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| Annotation | Half-map 1 of human SLC26A6 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Homodimer of the human SLC26A6 anion transporter
| Entire | Name: Homodimer of the human SLC26A6 anion transporter |
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| Components |
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-Supramolecule #1: Homodimer of the human SLC26A6 anion transporter
| Supramolecule | Name: Homodimer of the human SLC26A6 anion transporter / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Solute carrier family 26 member 6
| Macromolecule | Name: Solute carrier family 26 member 6 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 83.812328 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MSGLADASGP RDTQALLSAT QAMDLRRRDY HMERPLLNQE HLEELGRWGS APRTHQWRTW LQCSRARAYA LLLQHLPVLV WLPRYPVRD WLLGDLLSGL SVAIMQLPQG LAYALLAGLP PVFGLYSSFY PVFIYFLFGT SRHISVGTFA VMSVMVGSVT E SLAPQALN ...String: MSGLADASGP RDTQALLSAT QAMDLRRRDY HMERPLLNQE HLEELGRWGS APRTHQWRTW LQCSRARAYA LLLQHLPVLV WLPRYPVRD WLLGDLLSGL SVAIMQLPQG LAYALLAGLP PVFGLYSSFY PVFIYFLFGT SRHISVGTFA VMSVMVGSVT E SLAPQALN DSMINETARD AARVQVASTL SVLVGLFQVG LGLIHFGFVV TYLSEPLVRG YTTAAAVQVF VSQLKYVFGL HL SSHSGPL SLIYTVLEVC WKLPQSKVGT VVTAAVAGVV LVVVKLLNDK LQQQLPMPIP GELLTLIGAT GISYGMGLKH RFE VDVVGN IPAGLVPPVA PNTQLFSKLV GSAFTIAVVG FAIAISLGKI FALRHGYRVD SNQELVALGL SNLIGGIFQC FPVS CSMSR SLVQESTGGN SQVAGAISSL FILLIIVKLG ELFHDLPKAV LAAIIIVNLK GMLRQLSDMR SLWKANRADL LIWLV TFTA TILLNLDLGL VVAVIFSLLL VVVRTQMPHY SVLGQVPDTD IYRDVAEYSE AKEVRGVKVF RSSATVYFAN AEFYSD ALK QRCGVDVDFL ISQKKKLLKK QEQLKLKQLQ KEEKLRKQAA SPKGASVSIN VNTSLEDMRS NNVEDCKMMV SSGDKME DA TANGQEDSKA PDGSTLKALG LPQPDFHSLI LDLGALSFVD TVCLKSLKNI FHDFREIEVE VYMAACHSPV VSQLEAGH F FDASITKKHL FASVHDAVTF ALQHPRPVPD SPVSVTRLAL EVLFQ UniProtKB: Solute carrier family 26 member 6 |
-Macromolecule #2: CHLORIDE ION
| Macromolecule | Name: CHLORIDE ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: CL |
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| Molecular weight | Theoretical: 35.453 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 2 mg/mL | ||||||||||||
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| Buffer | pH: 7.4 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
| Vitrification | Cryogen name: ETHANE-PROPANE | ||||||||||||
| Details | Full-lengthed Human SLC26A6 expressed in HEK293S GNTi- cells |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 2 / Number real images: 11962 / Average electron dose: 67.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Switzerland, 1 items
Citation


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X (Row.)
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Processing
FIELD EMISSION GUN

