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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 / Proton/oligopeptide cotransporters / peptidoglycan transport / 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 / Proton/oligopeptide cotransporters / peptidoglycan transport / 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 / innate immune response / intracellular membrane-bounded organelle
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: Structure / Year: 2025
Title: The structures of the peptide transporters SLC15A3 and SLC15A4 reveal the recognition mechanisms for substrate and TASL.
Authors: Zhikuan Zhang / Shota Kasai / Kentaro Sakaniwa / Akiko Fujimura / Umeharu Ohto / Toshiyuki Shimizu /
Abstract: The solute carrier family 15 members 3 and 4 (SLC15A3 and SLC15A4) are closely related endolysosomal peptide transporters that transport free histidine and certain dipeptides from the lumen to ...The solute carrier family 15 members 3 and 4 (SLC15A3 and SLC15A4) are closely related endolysosomal peptide transporters that transport free histidine and certain dipeptides from the lumen to cytosol. Besides, SLC15A4 also functions as a scaffold protein for the recruitment of the adapter TASL for interferon regulatory factor 5 (IRF5) activation downstream of innate immune TLR7-9 signaling. However, the molecular basis for the substrate recognition and TASL recruitment by these membrane proteins is not well understood. Here, we report the cryoelectron microscopy (cryo-EM) structure of apo SLC15A3 and structures of SLC15A4 in the absence or presence of the substrate, revealing the specific dipeptide recognition mechanism. Each SLC15A3 and SLC15A4 protomer adopts an outward-facing conformation. Furthermore, we also present the cryo-EM structure of a SLC15A4-TASL complex. The N terminal region of TASL forms a helical structure that inserts deeply into the inward-facing cavity of SLC15A4.
History
DepositionOct 27, 2023-
Header (metadata) releaseDec 6, 2023-
Map releaseDec 6, 2023-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_37898.png

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
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 290 pix.
= 240.7 Å		0.83 Å/pix.
x 290 pix.
= 240.7 Å		0.83 Å/pix.
x 290 pix.
= 240.7 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
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

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_37898_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_37898_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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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

CTF correctionType: NONE
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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