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TitleStructural basis for multivitamin recognition and transport by human SMVT.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMay 16, 2026
AuthorsQiuxin Zhen / Mingshuai Wang / Zhe Zhang /
PubMed AbstractThe human sodium-dependent multivitamin transporter (SMVT, SLC5A6) mediates cellular uptake of essential metabolic cofactors, including biotin, pantothenate, and lipoate. Its dysfunction is ...The human sodium-dependent multivitamin transporter (SMVT, SLC5A6) mediates cellular uptake of essential metabolic cofactors, including biotin, pantothenate, and lipoate. Its dysfunction is associated with neurological disorders, metabolic abnormalities, and cancer. However, the molecular mechanism underlying its multi-substrate transport has remained elusive. Here, we present cryo-electron microscopy structures of human SMVT in three conformational states: occluded, outward-open, and inward-open. These structural snapshots capture the complete transport cycle and reveal a conserved substrate-binding pocket near a kinked transmembrane helix (TM1). Within this pocket, substrate carboxyl groups are electrostatically anchored, while distinct chemical moieties interact with specific polar and hydrophobic residues. Functional assays identify key binding residues and elucidate the pathogenic effects of disease-associated mutations. Further structural analysis delineates the principles of substrate discrimination within the SLC5 transporter family. Together, our work provides a structural framework for SMVT's polyspecificity and lays a foundation for understanding related diseases and developing targeted therapeutic strategies.
External linksNat Commun / PubMed:42364996
MethodsEM (single particle)
Resolution3.4 - 4.3 Å
Structure data

80903
EMDB Unreleased entry

26va

EMDB-80903, PDB-26va:
Biotin-bound SMVT in the occluded state
Method: EM (single particle) / Resolution: 3.4 Å

80904
EMDB Unreleased entry

26vb

EMDB-80904, PDB-26vb:
D-pantothenic acid-bound SMVT in the occluded state
Method: EM (single particle) / Resolution: 3.7 Å

80905
EMDB Unreleased entry

26vc

EMDB-80905, PDB-26vc:
Alpha-lipoic acid-bound SMVT in the occluded state
Method: EM (single particle) / Resolution: 4.1 Å

80906
EMDB Unreleased entry

26vd

EMDB-80906, PDB-26vd:
SMVT in the outward-open state
Method: EM (single particle) / Resolution: 4.3 Å

80907
EMDB Unreleased entry

26ve

EMDB-80907, PDB-26ve:
SMVT in the inward-open state
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-BTN:
BIOTIN

ChemComp-PAU:
PANTOTHENOIC ACID

ChemComp-LPA:
LIPOIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Sodium-dependent multivitamin transporter / SMVT / SLC5A6 / Biotin / D-pantothenic acid / Alpha-lipoic acid

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