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- EMDB-35949: Human ZnT1-D47N/D255N mutant -

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Basic information

Entry
Database: EMDB / ID: EMD-35949
TitleHuman ZnT1-D47N/D255N mutant
Map data
Sample
  • Complex: Human ZnT1-D47N/D255N mutant homodimer
    • Protein or peptide: Proton-coupled zinc antiporter SLC30A1
Keywordszinc exporter / TRANSPORT PROTEIN
Function / homology
Function and homology information


negative regulation of zinc ion transmembrane import / glutamatergic postsynaptic density / zinc export across plasma membrane / detoxification of zinc ion / detoxification of cadmium ion / zinc ion import into organelle / zinc:proton antiporter activity / Zinc efflux and compartmentalization by the SLC30 family / cadmium ion transmembrane transport / regulation of postsynaptic density protein 95 clustering ...negative regulation of zinc ion transmembrane import / glutamatergic postsynaptic density / zinc export across plasma membrane / detoxification of zinc ion / detoxification of cadmium ion / zinc ion import into organelle / zinc:proton antiporter activity / Zinc efflux and compartmentalization by the SLC30 family / cadmium ion transmembrane transport / regulation of postsynaptic density protein 95 clustering / zinc ion transport / negative regulation of neurotransmitter secretion / zinc ion transmembrane transporter activity / negative regulation of calcium ion import / zinc ion transmembrane transport / positive regulation of dendritic spine morphogenesis / intracellular zinc ion homeostasis / calcium ion import / postsynaptic density, intracellular component / calcium channel inhibitor activity / T-tubule / cytoplasmic vesicle membrane / postsynaptic density membrane / Schaffer collateral - CA1 synapse / intracellular calcium ion homeostasis / basolateral plasma membrane / nuclear membrane / in utero embryonic development / defense response to bacterium / Golgi membrane / dendrite / endoplasmic reticulum membrane / endoplasmic reticulum / Golgi apparatus / metal ion binding / membrane / plasma membrane / cytoplasm
Similarity search - Function
Cation efflux protein, cytoplasmic domain superfamily / Cation efflux protein / Cation efflux transmembrane domain superfamily / Cation efflux family
Similarity search - Domain/homology
Proton-coupled zinc antiporter SLC30A1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsSun L / Liu X / Sun C / He B
Funding support China, 1 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2020YFA0509302 China
CitationJournal: Sci Adv / Year: 2024
Title: Structural insights into the calcium-coupled zinc export of human ZnT1.
Authors: Chunqiao Sun / Bangguo He / Yongxiang Gao / Xingbing Wang / Xin Liu / Linfeng Sun /
Abstract: Cellular zinc (Zn) homeostasis is essential to human health and is under tight regulations. Human zinc transporter 1 (hZnT1) is a plasma membrane-localized Zn exporter belonging to the ZnT family, ...Cellular zinc (Zn) homeostasis is essential to human health and is under tight regulations. Human zinc transporter 1 (hZnT1) is a plasma membrane-localized Zn exporter belonging to the ZnT family, and its functional aberration is associated with multiple diseases. Here, we show that hZnT1 works as a Zn/Ca exchanger. We determine the structure of hZnT1 using cryo-electron microscopy (cryo-EM) single particle analysis. hZnT1 adopts a homodimeric structure, and each subunit contains a transmembrane domain consisting of six transmembrane segments, a cytosolic domain, and an extracellular domain. The transmembrane region displays an outward-facing conformation. On the basis of structural and functional analysis, we propose a model for the hZnT1-mediated Zn/Ca exchange. Together, these results facilitate our understanding of the biological functions of hZnT1 and provide a basis for further investigations of the ZnT family transporters.
History
DepositionApr 14, 2023-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_35949.png

Downloads & links

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Map

FileDownload / File: emd_35949.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 200 pix.
= 220. Å		1.1 Å/pix.
x 200 pix.
= 220. Å		1.1 Å/pix.
x 200 pix.
= 220. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.7
Minimum - Maximum-4.958342 - 7.3256483
Average (Standard dev.)0.009931077 (±0.14320028)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 220.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35949_half_map_1.map
Projections & Slices
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Half map: #2

Fileemd_35949_half_map_2.map
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Sample components

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Entire : Human ZnT1-D47N/D255N mutant homodimer

EntireName: Human ZnT1-D47N/D255N mutant homodimer
Components
  • Complex: Human ZnT1-D47N/D255N mutant homodimer
    • Protein or peptide: Proton-coupled zinc antiporter SLC30A1

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Supramolecule #1: Human ZnT1-D47N/D255N mutant homodimer

SupramoleculeName: Human ZnT1-D47N/D255N mutant homodimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Proton-coupled zinc antiporter SLC30A1

MacromoleculeName: Proton-coupled zinc antiporter SLC30A1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.360633 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGCWGRNRGR LLCMLALTFM FMVLEVVVSR VTSSLAMLSD SFHMLSNVLA LVVALVAERF ARRTHATQKN TFGWIRAEVM GALVNAIFL TGLCFAILLE AIERFIEPHE MQQPLVVLGV GVAGLLVNVL GLCLFHHHSG FSQDSGHGHS HGGHGHGHGL P KGPRVKST ...String:
MGCWGRNRGR LLCMLALTFM FMVLEVVVSR VTSSLAMLSD SFHMLSNVLA LVVALVAERF ARRTHATQKN TFGWIRAEVM GALVNAIFL TGLCFAILLE AIERFIEPHE MQQPLVVLGV GVAGLLVNVL GLCLFHHHSG FSQDSGHGHS HGGHGHGHGL P KGPRVKST RPGSSDINVA PGEQGPDQEE TNTLVANTSN SNGLKLDPAD PENPRSGDTV EVQVNGNLVR EPDHMELEED RA GQLNMRG VFLHVLGNAL GSVIVVVNAL VFYFSWKGCS EGDFCVNPCF PDPCKAFVEI INSTHASVYE AGPCWVLYLD PTL CVVMVC ILLYTTYPLL KESALILLQT VPKQIDIRNL IKELRNVEGV EEVHELHVWQ LAGSRIIATA HIKCEDPTSY MEVA KTIKD VFHNHGIHAT TIQPEFASVG SKSSVVPCEL ACRTQCALKQ CCGTLPQAPS GKDAEKTPAV SISCLELSNN LEKKP RRTK AENIPAVVIE IKNMPNKQPE SSL

UniProtKB: Proton-coupled zinc antiporter SLC30A1

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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: 7.4
GridModel: Quantifoil / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: DIFFRACTION / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 1.5 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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 550472
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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