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Structure paper

TitleMolecular mechanism of choline and ethanolamine transport in humans.
Journal, issue, pagesNature, Vol. 630, Issue 8016, Page 501-508, Year 2024
Publish dateMay 22, 2024
AuthorsKeiken Ri / Tsai-Hsuan Weng / Ainara Claveras Cabezudo / Wiebke Jösting / Yu Zhang / Andre Bazzone / Nancy C P Leong / Sonja Welsch / Raymond T Doty / Gonca Gursu / Tiffany Jia Ying Lim / Sarah Luise Schmidt / Janis L Abkowitz / Gerhard Hummer / Di Wu / Long N Nguyen / Schara Safarian /
PubMed AbstractHuman feline leukaemia virus subgroup C receptor-related proteins 1 and 2 (FLVCR1 and FLVCR2) are members of the major facilitator superfamily. Their dysfunction is linked to several clinical ...Human feline leukaemia virus subgroup C receptor-related proteins 1 and 2 (FLVCR1 and FLVCR2) are members of the major facilitator superfamily. Their dysfunction is linked to several clinical disorders, including PCARP, HSAN and Fowler syndrome. Earlier studies concluded that FLVCR1 may function as a haem exporter, whereas FLVCR2 was suggested to act as a haem importer, yet conclusive biochemical and detailed molecular evidence remained elusive for the function of both transporters. Here, we show that FLVCR1 and FLVCR2 facilitate the transport of choline and ethanolamine across the plasma membrane, using a concentration-driven substrate translocation process. Through structural and computational analyses, we have identified distinct conformational states of FLVCRs and unravelled the coordination chemistry underlying their substrate interactions. Fully conserved tryptophan and tyrosine residues form the binding pocket of both transporters and confer selectivity for choline and ethanolamine through cation-π interactions. Our findings clarify the mechanisms of choline and ethanolamine transport by FLVCR1 and FLVCR2, enhance our comprehension of disease-associated mutations that interfere with these vital processes and shed light on the conformational dynamics of these major facilitator superfamily proteins during the transport cycle.
External linksNature / PubMed:38778100 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.1 Å
Structure data

18334

8qcs

EMDB-18334, PDB-8qcs:
Cryo-EM structure of the inward-facing FLVCR1
Method: EM (single particle) / Resolution: 2.9 Å

18335

8qct

EMDB-18335, PDB-8qct:
Cryo-EM structure of the inward-facing choline-bound FLVCR1
Method: EM (single particle) / Resolution: 2.6 Å

18336

8qcx

EMDB-18336, PDB-8qcx:
Cryo-EM structure of the inward-facing FLVCR2
Method: EM (single particle) / Resolution: 3.1 Å

18337

8qcy

EMDB-18337, PDB-8qcy:
Cryo-EM structure of the outward-facing FLVCR2
Method: EM (single particle) / Resolution: 2.9 Å

18339

8qd0

EMDB-18339, PDB-8qd0:
Cryo-EM structure of the inward-facing choline-bound FLVCR2
Method: EM (single particle) / Resolution: 2.8 Å

19009

8r8t

EMDB-19009, PDB-8r8t:
Cryo-EM structure of the inward-facing ethanolamine-bound FLVCR1
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-CHT:
CHOLINE ION

ChemComp-ETA:
ETHANOLAMINE

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / MFS / choline / human transporter / choline transport / ethanolamine transport

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