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Literature summary for 3.5.1.52 extracted from

  • Zhao, G.; Zhou, X.; Wang, L.; Li, G.; Schindelin, H.; Lennarz, W.J.
    Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation (2007), Proc. Natl. Acad. Sci. USA, 104, 8785-8790.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion, crystal structure of the N-terminal domain of PNGase in complex with the cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus provides detailed insight into the interaction between p97 and its substrate-processing cofactors Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATPase p97 + H2O Mus musculus a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97’s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors ?
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Organism

Organism UniProt Comment Textmining
Mus musculus Q9JI78
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATPase p97 + H2O a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97’s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors Mus musculus ?
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 ?
ATPase p97 + H2O a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase Mus musculus ?
-
 ?