View source for 5mpe


==26S proteasome in presence of ATP (s2)==
<SX load='5mpe' size='340' side='right' viewer='molstar' caption='[[5mpe]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mpe]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MPE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mpe OCA], [https://pdbe.org/5mpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mpe RCSB], [https://www.ebi.ac.uk/pdbsum/5mpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mpe ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/RPN10_YEAST RPN10_YEAST] Multiubiquitin binding protein.
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== Publication Abstract from PubMed ==
In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for the regulated degradation of intracellular proteins. The 26S holocomplex comprises the core particle (CP), where proteolysis takes place, and one or two regulatory particles (RPs). The base of the RP is formed by a heterohexameric AAA+ ATPase module, which unfolds and translocates substrates into the CP. Applying single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states (s1 to s4). The resolution of the four conformers allowed for the construction of atomic models of the AAA+ ATPase module as it progresses through the functional cycle. In a hitherto unobserved state (s4), the gate controlling access to the CP is open. The structures described in this study allow us to put forward a model for the 26S functional cycle driven by ATP hydrolysis.

Structural insights into the functional cycle of the ATPase module of the 26S proteasome.,Wehmer M, Rudack T, Beck F, Aufderheide A, Pfeifer G, Plitzko JM, Forster F, Schulten K, Baumeister W, Sakata E Proc Natl Acad Sci U S A. 2017 Feb 7;114(6):1305-1310. doi:, 10.1073/pnas.1621129114. Epub 2017 Jan 23. PMID:28115689<ref>PMID:28115689</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5mpe" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Aufderheide A]]
[[Category: Baumeister W]]
[[Category: Beck F]]
[[Category: Foerster F]]
[[Category: Pfeifer G]]
[[Category: Plitzko JM]]
[[Category: Rudack T]]
[[Category: Sakata E]]
[[Category: Schulten K]]
[[Category: Wehmer M]]