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Structure paper

TitleStructural basis of regulated N-glycosylation at the secretory translocon
Journal, issue, pagesNature, Year 2025
Publish dateFeb 10, 2025 (structure data deposition date)
AuthorsYamsek M / Ma M / Jha R / Wan Y / Li Q / Zhong F / DeLong K / Ji Z / Rohatgi R / Keenan RJ
External linksNature / Search PubMed
MethodsEM (single particle)
Resolution3.2 - 4.1 Å
Structure data

49171

9n9j

EMDB-49171, PDB-9n9j:
Structure of a GRP94 folding intermediate engaged with a CCDC134- and FKBP11-bound secretory translocon
Method: EM (single particle) / Resolution: 3.2 Å

72945

9ygy

EMDB-72945, PDB-9ygy:
Structure of a GRP94 folding intermediate engaged with a CCDC134- and FKBP11-bound secretory translocon
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-ELU:
phosphono [(3~{R},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl] hydrogen phosphate

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsRIBOSOME / Membrane protein / Translocon / Transport / N-Glycosylation

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