Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
5.6.1.5	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

EC Number	Protein Variants	Comment	Organism
5.6.1.5	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

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.6.1.5	Methanocaldococcus jannaschii	-	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
5.6.1.5	PAN	-	Methanocaldococcus jannaschii

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Release 2023.1 (January 2023)