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	Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 111, Issue 15, Page 5544-5549, Year 2014
掲載日	2014年4月15日
著者	Pia Unverdorben / Florian Beck / Paweł Śledź / Andreas Schweitzer / Günter Pfeifer / Jürgen M Plitzko / Wolfgang Baumeister / Friedrich Förster /
PubMed 要旨	The 26S proteasome is a 2.5 MDa molecular machine that executes the degradation of substrates of the ubiquitin-proteasome pathway. The molecular architecture of the 26S proteasome was recently ...The 26S proteasome is a 2.5 MDa molecular machine that executes the degradation of substrates of the ubiquitin-proteasome pathway. The molecular architecture of the 26S proteasome was recently established by cryo-EM approaches. For a detailed understanding of the sequence of events from the initial binding of polyubiquitylated substrates to the translocation into the proteolytic core complex, it is necessary to move beyond static structures and characterize the conformational landscape of the 26S proteasome. To this end we have subjected a large cryo-EM dataset acquired in the presence of ATP and ATP-γS to a deep classification procedure, which deconvolutes coexisting conformational states. Highly variable regions, such as the density assigned to the largest subunit, Rpn1, are now well resolved and rendered interpretable. Our analysis reveals the existence of three major conformations: in addition to the previously described ATP-hydrolyzing (ATPh) and ATP-γS conformations, an intermediate state has been found. Its AAA-ATPase module adopts essentially the same topology that is observed in the ATPh conformation, whereas the lid is more similar to the ATP-γS bound state. Based on the conformational ensemble of the 26S proteasome in solution, we propose a mechanistic model for substrate recognition, commitment, deubiquitylation, and translocation into the core particle.
リンク	Proc Natl Acad Sci U S A / PubMed:24706844 / PubMed Central
手法	EM (単粒子)
解像度	7.7 - 9.3 Å
構造データ	2594 4cr2 EMDB-2594, PDB-4cr2: Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome 手法: EM (単粒子) / 解像度: 7.7 Å 2595 4cr3 EMDB-2595, PDB-4cr3: Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome 手法: EM (単粒子) / 解像度: 9.3 Å 2596 4cr4 EMDB-2596, PDB-4cr4: Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome 手法: EM (単粒子) / 解像度: 8.8 Å
由来	saccharomyces cerevisiae (パン酵母)
キーワード	HYDROLASE / AAA-ATPASE / ATP-ANALOG / CLASSIFICATION