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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 / zinc export across plasma membrane / detoxification of zinc ion / zinc ion import into organelle / detoxification of cadmium ion / zinc:proton antiporter activity / Zinc efflux and compartmentalization by the SLC30 family / cadmium ion transmembrane transport / zinc ion transmembrane transporter activity / zinc ion transport ...negative regulation of zinc ion transmembrane import / zinc export across plasma membrane / detoxification of zinc ion / zinc ion import into organelle / detoxification of cadmium ion / zinc:proton antiporter activity / Zinc efflux and compartmentalization by the SLC30 family / cadmium ion transmembrane transport / zinc ion transmembrane transporter activity / zinc ion transport / zinc ion transmembrane transport / negative regulation of calcium ion import / negative regulation of neurotransmitter secretion / intracellular zinc ion homeostasis / calcium ion import / calcium channel inhibitor activity / T-tubule / postsynaptic density membrane / Schaffer collateral - CA1 synapse / cytoplasmic vesicle membrane / intracellular calcium ion homeostasis / basolateral plasma membrane / nuclear membrane / in utero embryonic development / defense response to bacterium / Golgi apparatus / endoplasmic reticulum / metal ion binding / 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: To Be Published
Title: Structure of the human ZnT1-D47N/D255N double mutant
Authors: Sun L / Liu X / Sun C / He B
History
DepositionApr 14, 2023-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateApr 17, 2024-
Current statusApr 17, 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

Image control

Size
Brightness
Contrast
Others
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

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

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
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_35949_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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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
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
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 550472

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