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Literature summary for 5.6.1.5 extracted from

  • Yu, Y.; Smith, D.M.; Kim, H.M.; Rodriguez, V.; Goldberg, A.L.; Cheng, Y.
    Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions (2010), EMBO J., 29, 692-702.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN is determined. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S a-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
additional information six mutants of the PAN ATPases, in which PAN's seven C-terminal residues are replaced by the corresponding C-terminal residues of one of the yeast ATPases, Rpt1-Rpt6: Wild-type PAN and the PANRpt5 stimulate gate opening of the alpha3-alpha4 20S pocket mutant. None of the PANRpt mutants or wild-type PAN stimulate gate opening of 20S alpha1-alpha2 pocket mutant, and PANRpt2 stimulates gate opening of wild-type 20S, but not the alpha3-alpha4 pocket mutant. Only PANRpt5 is found to bind to one or both ends of the 20S alpha3-alpha4 pocket mutant, whereas none of the PANRpts forms a complex with the alpha1-alpha2 pocket mutant Methanocaldococcus jannaschii

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
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Synonyms

Synonyms Comment Organism
PAN
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Methanocaldococcus jannaschii