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	Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 111, Issue 15, Page 5544-5549, Year 2014
Publish date	Apr 15, 2014
Authors	Pia Unverdorben / Florian Beck / Paweł Śledź / Andreas Schweitzer / Günter Pfeifer / Jürgen M Plitzko / Wolfgang Baumeister / Friedrich Förster /
PubMed Abstract	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.
External links	Proc Natl Acad Sci U S A / PubMed:24706844 / PubMed Central
Methods	EM (single particle)
Resolution	7.7 - 9.3 Å
Structure data	2594 4cr2 EMDB-2594, PDB-4cr2: Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 8.8 Å
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	HYDROLASE / AAA-ATPASE / ATP-ANALOG / CLASSIFICATION