Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Reconfiguration of the proteasome during chaperone-mediated assembly.
Journal, issue, pages	Nature, Vol. 497, Issue 7450, Page 512-516, Year 2013
Publish date	May 23, 2013
Authors	Soyeon Park / Xueming Li / Ho Min Kim / Chingakham Ranjit Singh / Geng Tian / Martin A Hoyt / Scott Lovell / Kevin P Battaile / Michal Zolkiewski / Philip Coffino / Jeroen Roelofs / Yifan Cheng / Daniel Finley /
PubMed Abstract	The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting ...The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes, it inserts into the α2/α3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme.
External links	Nature / PubMed:23644457 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	5 - 9.6 Å
Structure data	EMDB-5593: 3D reconstruction of yeast 20S proteasome core particle Method: EM (single particle) / Resolution: 6.9 Å EMDB-5611: Yeast 20S proteasome with C-terminal peptide of yeast Rpt1 Method: EM (single particle) / Resolution: 7.3 Å EMDB-5612: Yeast 20S proteasome with C-terminal peptide of yeast Rpt2 Method: EM (single particle) / Resolution: 7.7 Å EMDB-5613: Yeast 20S proteasome with C-terminal peptide of yeast Rpt3 Method: EM (single particle) / Resolution: 7.7 Å EMDB-5614: Yeast 20S proteasome with C-terminal peptide of yeast Rpt4 Method: EM (single particle) / Resolution: 7.8 Å EMDB-5615: Yeast 20S proteasome with C-terminal peptide of yeast Rpt5 Method: EM (single particle) / Resolution: 8.1 Å EMDB-5616: Yeast 20S proteasome with C-terminal peptide of yeast Rpt1 Method: EM (single particle) / Resolution: 7.9 Å EMDB-5617: Yeast 20S proteasome in complex with purified yeast 19S base sub complex Method: EM (single particle) / Resolution: 9.6 Å PDB-4jpo: 5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1 Method: X-RAY DIFFRACTION / Resolution: 5 Å
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	CHAPERONE/HYDROLASE / Hsm3 / Chaperone / Proteasome / Protein Complex / CHAPERONE-HYDROLASE complex