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TitleStructural basis of lipid transfer by a bridge-like lipid-transfer protein.
Journal, issue, pagesNature, Vol. 642, Issue 8066, Page 242-249, Year 2025
Publish dateApr 23, 2025
AuthorsYunsik Kang / Katherine S Lehmann / Hannah Long / Amanda Jefferson / Maria Purice / Marc Freeman / Sarah Clark /
PubMed AbstractBridge-like lipid-transport proteins (BLTPs) are an evolutionarily conserved family of proteins that localize to membrane-contact sites and are thought to mediate the bulk transfer of lipids from a ...Bridge-like lipid-transport proteins (BLTPs) are an evolutionarily conserved family of proteins that localize to membrane-contact sites and are thought to mediate the bulk transfer of lipids from a donor membrane, typically the endoplasmic reticulum, to an acceptor membrane, such as that of the cell or an organelle. Although BLTPs are fundamentally important for a wide array of cellular functions, their architecture, composition and lipid-transfer mechanisms remain poorly characterized. Here we present the subunit composition and the cryogenic electron microscopy structure of the native LPD-3 BLTP complex isolated from transgenic Caenorhabditis elegans. LPD-3 folds into an elongated, rod-shaped tunnel of which the interior is filled with ordered lipid molecules that are coordinated by a track of ionizable residues that line one side of the tunnel. LPD-3 forms a complex with two previously uncharacterized proteins, one of which we have named Spigot and the other of which remains unnamed. Spigot interacts with the N-terminal end of LPD-3 where lipids are expected to enter the tunnel, and experiments in multiple model systems indicate that Spigot has a conserved role in BLTP function. Our LPD-3 complex structural data reveal protein-lipid interactions that suggest a model for how the native LPD-3 complex mediates bulk lipid transport and provides a foundation for mechanistic studies of BLTPs.
External linksNature / PubMed:40269155
MethodsEM (single particle)
Resolution2.7 - 6.2 Å
Structure data

EMDB-45276: Map of full-length LPD-3 complex
Method: EM (single particle) / Resolution: 6.2 Å

45399

9cap

EMDB-45399, PDB-9cap:
Structure of the LPD-3 complex
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

ChemComp-R16:
HEXADECANE

Source
  • caenorhabditis elegans (invertebrata)
KeywordsLIPID TRANSPORT / Native / membrane protein complex / BLTP

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