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- EMDB-37898: Cryo-EM structure of human SLC15A3 (dimer) -

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Basic information

Entry
Database: EMDB / ID: EMD-37898
TitleCryo-EM structure of human SLC15A3 (dimer)
Map dataB-factor sharpened map
Sample
  • Complex: Human SLC15A3
    • Protein or peptide: Solute carrier family 15 member 3
KeywordsTransporter / MEMBRANE PROTEIN
Function / homology
Function and homology information


peptidoglycan transmembrane transporter activity / peptidoglycan transport / Proton/oligopeptide cotransporters / dipeptide import across plasma membrane / peptide:proton symporter activity / dipeptide transmembrane transporter activity / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / monoatomic ion transport / protein transport / endosome membrane ...peptidoglycan transmembrane transporter activity / peptidoglycan transport / Proton/oligopeptide cotransporters / dipeptide import across plasma membrane / peptide:proton symporter activity / dipeptide transmembrane transporter activity / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / monoatomic ion transport / protein transport / endosome membrane / lysosomal membrane / intracellular membrane-bounded organelle / innate immune response
Similarity search - Function
Proton-dependent oligopeptide transporter family / POT family / MFS transporter superfamily
Similarity search - Domain/homology
Solute carrier family 15 member 3
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.44 Å
AuthorsKasai S / Zhang Z / Ohto U / Shimizu T
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Cryo-EM structure of human SLC15A3 (outward-facing partially occluded)
Authors: Zhang Z / Kasai S / Sakaniwa K / Fujimura A / Ohto U / Shimizu T
History
DepositionOct 27, 2023-
Header (metadata) releaseDec 6, 2023-
Map releaseDec 6, 2023-
UpdateMay 1, 2024-
Current statusMay 1, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_37898.map.gz / Format: CCP4 / Size: 93 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationB-factor sharpened map
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.27
Minimum - Maximum-0.93110484 - 1.4568214
Average (Standard dev.)0.0019335216 (±0.047066204)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions290290290
Spacing290290290
CellA=B=C: 240.7 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Unsharpened map

Fileemd_37898_additional_1.map
AnnotationUnsharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_37898_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_37898_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Human SLC15A3

EntireName: Human SLC15A3
Components
  • Complex: Human SLC15A3
    • Protein or peptide: Solute carrier family 15 member 3

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Supramolecule #1: Human SLC15A3

SupramoleculeName: Human SLC15A3 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Solute carrier family 15 member 3

MacromoleculeName: Solute carrier family 15 member 3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 67.140953 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSYYHHHHHH DYKDDDDKLE VLFQGPEFMP APRAREQPRV PGERQPLLPR GARGPRRWRR AAGAAVLLVE MLERAAFFGV TANLVLYLN STNFNWTGEQ ATRAALVFLG ASYLLAPVGG WLADVYLGRY RAVALSLLLY LAASGLLPAT AFPDGRSSFC G EMPASPLG ...String:
MSYYHHHHHH DYKDDDDKLE VLFQGPEFMP APRAREQPRV PGERQPLLPR GARGPRRWRR AAGAAVLLVE MLERAAFFGV TANLVLYLN STNFNWTGEQ ATRAALVFLG ASYLLAPVGG WLADVYLGRY RAVALSLLLY LAASGLLPAT AFPDGRSSFC G EMPASPLG PACPSAGCPR SSPSPYCAPV LYAGLLLLGL AASSVRSNLT SFGADQVMDL GRDATRRFFN WFYWSINLGA VL SLLVVAF IQQNISFLLG YSIPVGCVGL AFFIFLFATP VFITKPPMGS QVSSMLKLAL QNCCPQLWQR HSARDRQCAR VLA DERSPQ PGASPQEDIA NFQVLVKILP VMVTLVPYWM VYFQMQSTYV LQGLHLHIPN IFPANPANIS VALRAQGSSY TIPE AWLLL ANVVVVLILV PLKDRLIDPL LLRCKLLPSA LQKMALGMFF GFTSVIVAGV LEMERLHYIH HNETVSQQIG EVLYN AAPL SIWWQIPQYL LIGISEIFAS IPGLEFAYSE APRSMQGAIM GIFFCLSGVG SLLGSSLVAL LSLPGGWLHC PKDFGN INN CRMDLYFFLL AGIQAVTALL FVWIAGRYER ASQGPASHSR FSRDRG

UniProtKB: Solute carrier family 15 member 3

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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

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 56.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.44 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 91199
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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