View source for 4ady


==Crystal structure of 26S proteasome subunit Rpn2==
<StructureSection load='4ady' size='340' side='right'caption='[[4ady]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ady]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4ady FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ady OCA], [https://pdbe.org/4ady PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ady RCSB], [https://www.ebi.ac.uk/pdbsum/4ady PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ady ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPN2_YEAST RPN2_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.<ref>PMID:9584156</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 26S proteasome proteolyses ubiquitylated proteins and is assembled from a 20S proteolytic core and two 19S regulatory particles (19S-RP). The 19S-RP scaffolding subunits Rpn1 and Rpn2 function to engage ubiquitin receptors. Rpn1 and Rpn2 are characterized by eleven tandem copies of a 35-40 amino acid repeat motif termed the proteasome/cyclosome (PC) repeat. Here, we reveal that the eleven PC repeats of Rpn2 form a closed toroidal structure incorporating two concentric rings of alpha helices encircling two axial alpha helices. A rod-like N-terminal domain consisting of 17 stacked alpha helices and a globular C-terminal domain emerge from one face of the toroid. Rpn13, an ubiquitin receptor, binds to the C-terminal 20 residues of Rpn2. Rpn1 adopts a similar conformation to Rpn2 but differs in the orientation of its rod-like N-terminal domain. These findings have implications for understanding how 19S-RPs recognize, unfold, and deliver ubiquitylated substrates to the 20S core.

The Structure of the 26S Proteasome Subunit Rpn2 Reveals Its PC Repeat Domain as a Closed Toroid of Two Concentric alpha-Helical Rings.,He J, Kulkarni K, da Fonseca PC, Krutauz D, Glickman MH, Barford D, Morris EP Structure. 2012 Mar 7;20(3):513-21. PMID:22405010<ref>PMID:22405010</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ady" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Barford D]]
[[Category: Da Fonseca PCA]]
[[Category: Glickman MH]]
[[Category: He J]]
[[Category: Krutauz D]]
[[Category: Kulkarni K]]
[[Category: Morris EP]]