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- EMDB-32561: Mouse Pendrin bound bicarbonate in inward state -

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Basic information

Entry
Database: EMDB / ID: EMD-32561
TitleMouse Pendrin bound bicarbonate in inward state
Map data
Sample
  • Complex: mouse Pendrin bound bicarbonate in inward state
    • Protein or peptide: Pendrin
  • Ligand: BICARBONATE ION
Keywordsexchange / transport / slc / TRANSPORT PROTEIN
Function / homology
Function and homology information


Multifunctional anion exchangers / inorganic anion transport / iodide transmembrane transporter activity / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / monoatomic anion transmembrane transporter activity / regulation of pH / chloride:bicarbonate antiporter activity / bicarbonate transmembrane transporter activity ...Multifunctional anion exchangers / inorganic anion transport / iodide transmembrane transporter activity / sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / monoatomic anion transmembrane transporter activity / regulation of pH / chloride:bicarbonate antiporter activity / bicarbonate transmembrane transporter activity / chloride transmembrane transporter activity / animal organ morphogenesis / brush border membrane / regulation of protein localization / apical plasma membrane / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Sulphate anion transporter, conserved site / SLC26A transporters signature. / SLC26A/SulP transporter / SLC26A/SulP transporter domain / Sulfate permease family / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.49 Å
AuthorsLiu QY / Zhang X / Sun L / Chen ZG
Funding support1 items
OrganizationGrant numberCountry
Not funded81900729
CitationJournal: Nat Commun / Year: 2023
Title: Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.
Authors: Qianying Liu / Xiang Zhang / Hui Huang / Yuxin Chen / Fang Wang / Aihua Hao / Wuqiang Zhan / Qiyu Mao / Yuxia Hu / Lin Han / Yifang Sun / Meng Zhang / Zhimin Liu / Geng-Lin Li / Weijia Zhang ...Authors: Qianying Liu / Xiang Zhang / Hui Huang / Yuxin Chen / Fang Wang / Aihua Hao / Wuqiang Zhan / Qiyu Mao / Yuxia Hu / Lin Han / Yifang Sun / Meng Zhang / Zhimin Liu / Geng-Lin Li / Weijia Zhang / Yilai Shu / Lei Sun / Zhenguo Chen /
Abstract: Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing ...Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However its molecular structure has remained unknown, limiting our understanding of the structural basis of transport. Here, we determine the cryo-electron microscopy structures of mouse pendrin with symmetric and asymmetric homodimer conformations. The asymmetric homodimer consists of one inward-facing protomer and the other outward-facing protomer, representing coincident uptake and secretion- a unique state of pendrin as an electroneutral exchanger. The multiple conformations presented here provide an inverted alternate-access mechanism for anion exchange. The structural and functional data presented here disclose the properties of an anion exchange cleft and help understand the importance of disease-associated variants, which will shed light on the pendrin exchange mechanism.
History
DepositionJan 8, 2022-
Header (metadata) releaseMay 17, 2023-
Map releaseMay 17, 2023-
UpdateAug 16, 2023-
Current statusAug 16, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32561.png

Downloads & links

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Map

FileDownload / File: emd_32561.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 320 pix.
= 334.72 Å		1.05 Å/pix.
x 320 pix.
= 334.72 Å		1.05 Å/pix.
x 320 pix.
= 334.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.046 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0001
Minimum - Maximum-0.0031160503 - 1.6173308
Average (Standard dev.)0.0007140157 (±0.01885235)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 334.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : mouse Pendrin bound bicarbonate in inward state

EntireName: mouse Pendrin bound bicarbonate in inward state
Components
  • Complex: mouse Pendrin bound bicarbonate in inward state
    • Protein or peptide: Pendrin
  • Ligand: BICARBONATE ION

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Supramolecule #1: mouse Pendrin bound bicarbonate in inward state

SupramoleculeName: mouse Pendrin bound bicarbonate in inward state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Pendrin

MacromoleculeName: Pendrin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 85.769578 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAARGGRSEP PQLAEYSCSY TVSRPVYSEL AFQQQRERRL PERRTLRDSL ARSCSCSRKR AFGVVKTLLP ILDWLPKYRV KEWLLSDII SGVSTGLVGT LQGMAYALLA AVPVQFGLYS AFFPILTYFV FGTSRHISVG PFPVVSLMVG SVVLSMAPDD H FLVPSGNG ...String:
MAARGGRSEP PQLAEYSCSY TVSRPVYSEL AFQQQRERRL PERRTLRDSL ARSCSCSRKR AFGVVKTLLP ILDWLPKYRV KEWLLSDII SGVSTGLVGT LQGMAYALLA AVPVQFGLYS AFFPILTYFV FGTSRHISVG PFPVVSLMVG SVVLSMAPDD H FLVPSGNG SALNSTTLDT GTRDAARVLL ASTLTLLVGI IQLVFGGLQI GFIVRYLADP LVGGFTTAAA FQVLVSQLKI VL NVSTKNY NGILSIIYTL IEIFQNIGDT NIADFIAGLL TIIVCMAVKE LNDRFKHRIP VPIPIEVIVT IIATAISYGA NLE KNYNAG IVKSIPSGFL PPVLPSVGLF SDMLAASFSI AVVAYAIAVS VGKVYATKHD YVIDGNQEFI AFGISNVFSG FFSC FVATT ALSRTAVQES TGGKTQVAGL ISAVIVMVAI VALGRLLEPL QKSVLAAVVI ANLKGMFMQV CDVPRLWKQN KTDAV IWVF TCIMSIILGL DLGLLAGLLF ALLTVVLRVQ FPSWNGLGSV PSTDIYKSIT HYKNLEEPEG VKILRFSSPI FYGNVD GFK KCINSTVGFD AIRVYNKRLK ALRRIQKLIK KGQLRATKNG IISDIGSSNN AFEPDEDVEE PEELNIPTKE IEIQVDW NS ELPVKVNVPK VPIHSLVLDC GAVSFLDVVG VRSLRMIVKE FQRIDVNVYF ALLQDDVLEK MEQCGFFDDN IRKDRFFL T VHDAILHLQN QVKSREGQDS LLETVARIRD CKDPLDLMEA EMNAEELDVQ DEAMRRLAS

UniProtKB: Pendrin

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Macromolecule #2: BICARBONATE ION

MacromoleculeName: BICARBONATE ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: BCT
Molecular weightTheoretical: 61.017 Da
Chemical component information

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 53.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.49 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 134404
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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