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TitleInteractions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.
Journal, issue, pagesEMBO J, Vol. 29, Issue 3, Page 692-702, Year 2010
Publish dateFeb 3, 2010
AuthorsYadong Yu / David M Smith / Ho Min Kim / Victor Rodriguez / Alfred L Goldberg / Yifan Cheng /
PubMed AbstractProtein degradation in the 20S proteasome is regulated in eukaryotes by the 19S ATPase complex and in archaea by the homologous PAN ATPase ring complex. Subunits of these hexameric ATPases contain on ...Protein degradation in the 20S proteasome is regulated in eukaryotes by the 19S ATPase complex and in archaea by the homologous PAN ATPase ring complex. Subunits of these hexameric ATPases contain on their C-termini a conserved hydrophobic-tyrosine-X (HbYX) motif that docks into pockets in the 20S to stimulate the opening of a gated substrate entry channel. Here, we report the crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S alpha-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif. This structure together with related mutagenesis data suggest how in eukaryotes certain proteasomal ATPases bind to specific pockets in an asymmetrical manner to regulate gate opening.
External linksEMBO J / PubMed:20019667 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution4 - 7.5 Å
Structure data

EMDB-5130:
3D cryo-EM Structure of Archaeal 20S Proteasome in Complex with the C-terminus of PAN
Method: EM (single particle) / Resolution: 7.5 Å

PDB-3ipm:
Crystal Structure of Archaeal 20S Proteasome in Complex with the C-terminus of PAN
Method: X-RAY DIFFRACTION / Resolution: 4 Å

Source
  • thermoplasma acidophilum (acidophilic)
  • trypanosoma brucei brucei (eukaryote)
  • methanocaldococcus jannaschii (archaea)
KeywordsHYDROLASE/HYDROLASE ACTIVATOR / Proteasome / proteasomal ATPase / protein degradation / AAA ATPase / electron cryomicroscopy / Hydrolase / Protease / Threonine protease / HYDROLASE-HYDROLASE ACTIVATOR COMPLEX

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