4ady: Difference between revisions
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New page: '''Unreleased structure''' The entry 4ady is ON HOLD Authors: Kulkarni, K., He, J., daFonseca, P.C.A., Krutauz, D., Glickman, M.H., Barford, D., Morris, E.P. Description: Crystal struc... |
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The | ==Crystal structure of 26S proteasome subunit Rpn2== | ||
<StructureSection load='4ady' size='340' side='right'caption='[[4ady]], [[Resolution|resolution]] 2.70Å' 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]] 2.7Å</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®/PubMed®, 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]] | |||
