Journal
EMBO JOURNAL
Volume 29, Issue 3, Pages 692-702Publisher
WILEY
DOI: 10.1038/emboj.2009.382
Keywords
cryoelectron microscopy; proteasomal ATPase; proteasome; protein degradation; X-ray crystallography
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Funding
- NIH through the National Center for Research Resources' [PR17573, R01GM082893]
- UCSF Program for Breakthrough Biomedical Research
- NIGMS [R01GM51923-13]
- Multiple Myeloma Foundation
- Johnson & Johnson Foundation
- Medical Foundation
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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 a-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. The EMBO Journal (2010) 29, 692-702. doi:10.1038/emboj.2009.382; Published online 17 December 2009
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