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TitleNucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing.
Journal, issue, pagesImmunity, Vol. 58, Issue 9, Page 2166-22175.e4, Year 2025
Publish dateSep 9, 2025
AuthorsJames Lee / Victor Manon / Jue Chen /
PubMed AbstractThe transporter associated with antigen processing (TAP) delivers peptide antigens from the cytoplasm into the endoplasmic reticulum (ER) for loading onto major histocompatibility complex class I ...The transporter associated with antigen processing (TAP) delivers peptide antigens from the cytoplasm into the endoplasmic reticulum (ER) for loading onto major histocompatibility complex class I (MHC-I) molecules. To examine the mechanisms of peptide transport and release into the ER, we determined cryo-electron microscopy structures of the human TAP heterodimer in multiple functional states along the transport cycle. In the inward-facing conformation, when the peptide translocation cavity within the TAP heterodimer is exposed to the cytosol, ATP binding strengthened intradomain assembly. Transition to the outward-facing conformation, when the transporter opens to the ER lumen, led to a complete reconfiguration of the peptide-binding site, facilitating peptide release. ATP hydrolysis opened the catalytically active nucleotide-binding consensus site, and the subsequent separation of the nucleotide-binding domains reset the transport cycle. These findings establish a comprehensive structural framework for understanding unilateral peptide transport, vanadate trapping, and trans-inhibition-an internal feedback mechanism that prevents excessive peptide accumulation and activation of the ER stress response.
External linksImmunity / PubMed:40885191 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.7 Å
Structure data

49045

9n61

EMDB-49045, PDB-9n61:
Transporter associated with antigen processing (TAP) bound to the 9-mer peptide RRYQKSTEL and ATP
Method: EM (single particle) / Resolution: 3.6 Å

49046

9n62

EMDB-49046, PDB-9n62:
Transporter associated with antigen processing (TAP) EQ mutant bound to ATP in the inward-facing state
Method: EM (single particle) / Resolution: 3.4 Å

49047

9n63

EMDB-49047, PDB-9n63:
Transporter associated with antigen processing (TAP) EQ mutant bound to ATP in the outward-facing open state
Method: EM (single particle) / Resolution: 3.1 Å

49048

9n64

EMDB-49048, PDB-9n64:
Transporter associated with antigen processing (TAP) EQ mutant bound to ATP in the outward-facing kinked state
Method: EM (single particle) / Resolution: 3.7 Å

49049

9n65

EMDB-49049, PDB-9n65:
Transporter associated with antigen processing (TAP) bound to ATP and ADP In the inward-facing conformation
Method: EM (single particle) / Resolution: 3.7 Å

49050

9n66

EMDB-49050, PDB-9n66:
Transporter associated with antigen processing (TAP) bound to ATP and ADP in the outward-facing open state
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ABC transporter / antigen processing / peptide transporter

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