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- EMDB-52173: Human monocarboxylate transporter 10 -

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Basic information

Entry
Database: EMDB / ID: EMD-52173
TitleHuman monocarboxylate transporter 10
Map data
Sample
  • Organelle or cellular component: Human monocarboxylate transporter 10
    • Protein or peptide: Monocarboxylate transporter 10
KeywordsSLC16 / MSF / Transporter / MEMBRANE PROTEIN
Function / homology
Function and homology information


L-tyrosine transmembrane transporter activity / L-phenylalanine transmembrane transporter activity / aromatic amino acid transport / thyroid-stimulating hormone secretion / L-tryptophan transmembrane transporter activity / aromatic amino acid transmembrane transporter activity / thyroid hormone transmembrane transporter activity / thyroid hormone transport / Amino acid transport across the plasma membrane / amino acid transmembrane transporter activity ...L-tyrosine transmembrane transporter activity / L-phenylalanine transmembrane transporter activity / aromatic amino acid transport / thyroid-stimulating hormone secretion / L-tryptophan transmembrane transporter activity / aromatic amino acid transmembrane transporter activity / thyroid hormone transmembrane transporter activity / thyroid hormone transport / Amino acid transport across the plasma membrane / amino acid transmembrane transporter activity / thyroid hormone generation / amino acid transport / transmembrane transporter activity / cell junction / basolateral plasma membrane / intracellular membrane-bounded organelle / plasma membrane
Similarity search - Function
: / Major facilitator superfamily / Major Facilitator Superfamily / Major facilitator superfamily domain / Major facilitator superfamily (MFS) profile. / MFS transporter superfamily
Similarity search - Domain/homology
Monocarboxylate transporter 10
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsNordlin KP / Bagenholm V / Gourdon PE
Funding support Denmark, 1 items
OrganizationGrant numberCountry
Novo Nordisk Foundation0078574 Denmark
CitationJournal: Structure / Year: 2025
Title: Cryo-EM structure of the human monocarboxylate transporter 10.
Authors: Viktoria Bågenholm / Karl Patric Nordlin / Andrea Pasquadibisceglie / Andrey Belinskiy / Caroline Marcher Holm / Hajira Ahmed Hotiana / Kamil Gotfryd / Lucie Delemotte / Hussam Hassan Nour- ...Authors: Viktoria Bågenholm / Karl Patric Nordlin / Andrea Pasquadibisceglie / Andrey Belinskiy / Caroline Marcher Holm / Hajira Ahmed Hotiana / Kamil Gotfryd / Lucie Delemotte / Hussam Hassan Nour-Eldin / Per Amstrup Pedersen / Pontus Gourdon /
Abstract: The monocarboxylate transporter (MCT) membrane protein family has 14 human members that perform key cellular functions, such as regulating metabolism. MCT8 and MCT10 have unique cargo specificity, ...The monocarboxylate transporter (MCT) membrane protein family has 14 human members that perform key cellular functions, such as regulating metabolism. MCT8 and MCT10 have unique cargo specificity, transporting thyroid hormone and, in the case of MCT10, aromatic amino acids. Dysfunctional MCT8 causes the severe Allan-Herndon-Dudley syndrome, yet the (patho)physiology and function of MCT8 and MCT10 are not clearly understood, especially at a structural level. We present the cryoelectron microscopy (cryo-EM) structure of MCT10, displaying the classical major facilitator superfamily fold, caught in an inward-open configuration. Together with cargo docking models, the outward-open MCT10 AlphaFold model and validating functional analysis, cargo specificity and transport principles are proposed. These findings significantly enhance our understanding of the structure and function of MCTs, information that also may be valuable for the development of novel treatments against MCT-related disorders to address global challenges such as diabetes, obesity, and cancer.
History
DepositionNov 22, 2024-
Header (metadata) releaseMar 26, 2025-
Map releaseMar 26, 2025-
UpdateMay 14, 2025-
Current statusMay 14, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52173.png

Downloads & links

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Map

FileDownload / File: emd_52173.map.gz / Format: CCP4 / Size: 18.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.95 Å/pix.
x 168 pix.
= 159.5 Å		0.95 Å/pix.
x 168 pix.
= 159.5 Å		0.95 Å/pix.
x 168 pix.
= 159.5 Å

Surface

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Slices (1/2)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.9494 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.008
Minimum - Maximum-0.011790725 - 0.021660795
Average (Standard dev.)0.000015881365 (±0.0008443717)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions168168168
Spacing168168168
CellA=B=C: 159.50002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Unfiltered half map 1

Fileemd_52173_half_map_1.map
AnnotationUnfiltered half map 1
Projections & Slices
AxesZYX

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Half map: Unfiltered half map 2

Fileemd_52173_half_map_2.map
AnnotationUnfiltered half map 2
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Sample components

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Entire : Human monocarboxylate transporter 10

EntireName: Human monocarboxylate transporter 10
Components
  • Organelle or cellular component: Human monocarboxylate transporter 10
    • Protein or peptide: Monocarboxylate transporter 10

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Supramolecule #1: Human monocarboxylate transporter 10

SupramoleculeName: Human monocarboxylate transporter 10 / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Monocarboxylate transporter 10

MacromoleculeName: Monocarboxylate transporter 10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.537277 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MVLSQEEPDS ARGTSEAQPL GPAPTGAAPP PGPGPSDSPE AAVEKVEVEL AGPATAEPHE PPEPPEGGWG WLVMLAAMWC NGSVFGIQN ACGVLFVSML ETFGSKDDDK MVFKTAWVGS LSMGMIFFCC PIVSVFTDLF GCRKTAVVGA AVGFVGLMSS S FVSSIEPL ...String:
MVLSQEEPDS ARGTSEAQPL GPAPTGAAPP PGPGPSDSPE AAVEKVEVEL AGPATAEPHE PPEPPEGGWG WLVMLAAMWC NGSVFGIQN ACGVLFVSML ETFGSKDDDK MVFKTAWVGS LSMGMIFFCC PIVSVFTDLF GCRKTAVVGA AVGFVGLMSS S FVSSIEPL YLTYGIIFAC GCSFAYQPSL VILGHYFKKR LGLVNGIVTA GSSVFTILLP LLLRVLIDSV GLFYTLRVLC IF MFVLFLA GFTYRPLATS TKDKESGGSG SSLFSRKKFS PPKKIFNFAI FKVTAYAVWA VGIPLALFGY FVPYVHLMKH VNE RFQDEK NKEVVLMCIG VTSGVGRLLF GRIADYVPGV KKVYLQVLSF FFIGLMSMMI PLCSIFGALI AVCLIMGLFD GCFI SIMAP IAFELVGAQD VSQAIGFLLG FMSIPMTVGP PIAGLLRDKL GSYDVAFYLA GVPPLIGGAV LCFIPWIHSK KQREI SKTT GKEKMEKMLE NQNSLLSSSS GMFKKESDSI I

UniProtKB: Monocarboxylate transporter 10

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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

Concentration2.8 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 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 reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 195209
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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