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TitleLetA defines a structurally distinct transporter family.
Journal, issue, pagesNature, Year 2026
Publish dateJan 21, 2026
AuthorsCristina C Santarossa / Yupeng Li / Sara Yousef / Hale S Hasdemir / Carlos C Rodriguez / Max A B Haase / Minkyung Baek / Nicolas Coudray / John G Pavek / Kimber N Focke / Annika L Silverberg / Carmelita Bautista / Johannes T-H Yeh / Michael T Marty / David Baker / Emad Tajkhorshid / Damian C Ekiert / Gira Bhabha /
PubMed AbstractMembrane transport proteins translocate diverse cargos, ranging from small sugars to entire proteins, across cellular membranes. A few structurally distinct protein families have been described that ...Membrane transport proteins translocate diverse cargos, ranging from small sugars to entire proteins, across cellular membranes. A few structurally distinct protein families have been described that account for most of the known membrane transport processes. However, many membrane proteins with predicted transporter functions remain uncharacterized. Here we determined the structure of Escherichia coli LetAB, a phospholipid transporter involved in outer membrane integrity, and found that LetA adopts a distinct architecture that is structurally and evolutionarily unrelated to known transporter families. LetA localizes to the inner membrane, where it is poised to load lipids into its binding partner, LetB, a mammalian cell entry (MCE) protein that forms an approximately 225 Å long tunnel for lipid transport across the cell envelope. Unexpectedly, the LetA transmembrane domains adopt a fold that is evolutionarily related to the eukaryotic tetraspanin family of membrane proteins, including transmembrane AMPA receptor regulatory proteins (TARPs) and claudins. Through a combination of deep mutational scanning, molecular dynamics simulations, AlphaFold-predicted alternative states and functional studies, we present a model for how the LetA-like family of membrane transporters facilitates the transport of lipids across the bacterial cell envelope.
External linksNature / PubMed:41565823
MethodsEM (single particle)
Resolution3.5 Å
Structure data

49148

9n8w

EMDB-49148: Intermembrane lipid transport complex LetAB from Escherichia coli (Crosslinked, Composite Map 1)
PDB-9n8w: Intermembrane lipid transport complex LetAB from Escherichia coli (Crosslinked, Composite model corresponding to Map 1)
Method: EM (single particle) / Resolution: 3.5 Å

49152

9n8x

EMDB-49152: Intermembrane lipid transport complex LetAB from Escherichia coli (Composite Map 2)
PDB-9n8x: Intermembrane lipid transport complex LetAB from Escherichia coli (Composite model corresponding to Map 2)
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PEF:
DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • escherichia coli (E. coli)
  • escherichia coli str. k-12 substr. mg1655 (bacteria)
KeywordsLIPID TRANSPORT / Lipid transporter / Outer membrane integrity / MCE system / Metal-binding protein / Intermembrane complex

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