3IPM

Crystal Structure of Archaeal 20S Proteasome in Complex with the C-terminus of PAN

Summary for 3IPM

• Entry DOI: 10.2210/pdb3ipm/pdb
• EMDB information: 5130
• Descriptor: Proteasome subunit alpha, Proteasome subunit beta, Proteasome activator PA26, Proteasome-activating nucleotidase fusion protein (3 entities in total)
• Functional Keywords: proteasome, proteasomal atpase, protein degradation, aaa atpase, electron cryomicroscopy, hydrolase, protease, threonine protease, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• Biological source: Thermoplasma acidophilum; More
• Cellular location: Cytoplasm : P25156 P28061 Q58576
• Total number of polymer chains: 21
• Total formula weight: 533092.91

Authors

Yu, Y.,Cheng, Y. (deposition date: 2009-08-17, release date: 2009-12-29, Last modification date: 2023-09-06)

Primary citation

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.
Embo J., 29:692-702, 2010

PubMed Abstract: 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.

PubMed: 20019667
DOI: 10.1038/emboj.2009.382

Experimental method

X-RAY DIFFRACTION (4 Å)