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Structure paper

TitleCornichon receptors couple membrane adaptation to cargo selection during ER export
Journal, issue, pagesTo Be Published
Publish dateJul 20, 2026 (structure data deposition date)
AuthorsTunyi J / Adams O / Forrest L / Parker JL / Newstead S
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.76 - 2.85 Å
Structure data

59064

32pz

EMDB-59064, PDB-32pz:
Cryo-EM structure of Saccharomyces cerevisiae Erv14-Qdr2 complex in detergent
Method: EM (single particle) / Resolution: 2.83 Å

59065

32qa

EMDB-59065, PDB-32qa:
Cryo-EM structure of Saccharomyces cerevisiae Erv14-Qdr2 complex in lipid nanodiscs (double Erv14 assembly)
Method: EM (single particle) / Resolution: 2.76 Å

59066

32qb

EMDB-59066, PDB-32qb:
Cryo-EM structure of Saccharomyces cerevisiae Erv14-Qdr2 complex in lipid nanodiscs (single Erv14 assembly)
Method: EM (single particle) / Resolution: 2.85 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-ERG:
ERGOSTEROL

ChemComp-NKN:
(2R)-2-hydroxy-3-(phosphonooxy)propyl tetradecanoate

ChemComp-NKP:
(2R)-2-hydroxy-3-(phosphonooxy)propyl (9E)-octadec-9-enoate

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMEMBRANE PROTEIN / Cargo Receptor / Cornichon / Major Facilitator Superfamily / Drug:Proton Antiporter / Erv14 / Qdr2 / Lipid-Mediated Interface

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