EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Reconfiguration of the proteasome during chaperone-mediated assembly.
ジャーナル・号・ページ	Nature, Vol. 497, Issue 7450, Page 512-516, Year 2013
掲載日	2013年5月23日
著者	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 要旨	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.
リンク	Nature / PubMed:23644457 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	5 - 9.6 Å
構造データ	EMDB-5593: 3D reconstruction of yeast 20S proteasome core particle 手法: EM (単粒子) / 解像度: 6.9 Å EMDB-5611: Yeast 20S proteasome with C-terminal peptide of yeast Rpt1 手法: EM (単粒子) / 解像度: 7.3 Å EMDB-5612: Yeast 20S proteasome with C-terminal peptide of yeast Rpt2 手法: EM (単粒子) / 解像度: 7.7 Å EMDB-5613: Yeast 20S proteasome with C-terminal peptide of yeast Rpt3 手法: EM (単粒子) / 解像度: 7.7 Å EMDB-5614: Yeast 20S proteasome with C-terminal peptide of yeast Rpt4 手法: EM (単粒子) / 解像度: 7.8 Å EMDB-5615: Yeast 20S proteasome with C-terminal peptide of yeast Rpt5 手法: EM (単粒子) / 解像度: 8.1 Å EMDB-5616: Yeast 20S proteasome with C-terminal peptide of yeast Rpt1 手法: EM (単粒子) / 解像度: 7.9 Å EMDB-5617: Yeast 20S proteasome in complex with purified yeast 19S base sub complex 手法: EM (単粒子) / 解像度: 9.6 Å PDB-4jpo: 5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1 手法: X-RAY DIFFRACTION / 解像度: 5 Å
由来	saccharomyces cerevisiae (パン酵母)
キーワード	CHAPERONE/HYDROLASE / Hsm3 / Chaperone / Proteasome / Protein Complex / CHAPERONE-HYDROLASE complex