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- PDB-9hhq: Human monocarboxylate transporter 10 -

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Basic information

Entry
Database: PDB / ID: 9hhq
TitleHuman monocarboxylate transporter 10
ComponentsMonocarboxylate transporter 10
KeywordsMEMBRANE PROTEIN / SLC16 / MSF / Transporter
Function / homology
Function and homology information


L-tyrosine transmembrane transporter activity / L-phenylalanine transmembrane transporter activity / aromatic amino acid transport / thyroid-stimulating hormone secretion / monocarboxylic acid transmembrane transporter activity / L-tryptophan transmembrane transporter activity / thyroid hormone transmembrane transporter activity / aromatic amino acid transmembrane transporter activity / thyroid hormone transport / amino acid transmembrane transporter activity ...L-tyrosine transmembrane transporter activity / L-phenylalanine transmembrane transporter activity / aromatic amino acid transport / thyroid-stimulating hormone secretion / monocarboxylic acid transmembrane transporter activity / L-tryptophan transmembrane transporter activity / thyroid hormone transmembrane transporter activity / aromatic amino acid transmembrane transporter activity / thyroid hormone transport / amino acid transmembrane transporter activity / Amino acid transport across the plasma membrane / thyroid hormone generation / amino acid transport / 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)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsNordlin, K.P. / Bagenholm, V. / Gourdon, P.E.
Funding support Denmark, 1items
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, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 26, 2025Provider: repository / Type: Initial release
Revision 1.1Apr 2, 2025Group: Data collection / Database references / Category: citation / em_admin
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Monocarboxylate transporter 10


Theoretical massNumber of molelcules
Total (without water)55,5371
Polymers55,5371
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Monocarboxylate transporter 10 / MCT 10 / Aromatic amino acid transporter 1 / Solute carrier family 16 member 10 / T-type amino acid ...MCT 10 / Aromatic amino acid transporter 1 / Solute carrier family 16 member 10 / T-type amino acid transporter 1


Mass: 55537.277 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC16A10, MCT10, TAT1 / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: Q8TF71
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Human monocarboxylate transporter 10 / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Saccharomyces cerevisiae (brewer's yeast)
Buffer solutionpH: 8
SpecimenConc.: 2.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 700 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.21.1_5286: / Category: model refinement
CTF correctionType: NONE
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 195209 / Symmetry type: POINT

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