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The | ==Crystal structure of S. pombe Rpn12== | ||
<StructureSection load='4b0z' size='340' side='right'caption='[[4b0z]], [[Resolution|resolution]] 1.58Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b0z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B0Z 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]] 1.585Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</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=4b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b0z OCA], [https://pdbe.org/4b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b0z RCSB], [https://www.ebi.ac.uk/pdbsum/4b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b0z ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ubiquitin proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. We report the crystal structure of Rpn12, a proteasomal PCI- domain containing protein. The structure helps to define a core structural motif for the PCI-domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo. | |||
Structural and functional characterisation of Rpn12 identifies residues required for Rpn10 proteasome incorporation.,Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA Biochem J. 2012 Aug 20. PMID:22906049<ref>PMID:22906049</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4b0z" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Proteasome 3D structures|Proteasome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schizosaccharomyces pombe]] | |||
[[Category: Boehringer J]] | |||
[[Category: Endicott JA]] | |||
[[Category: Gordon C]] | |||
[[Category: Johnson EOD]] | |||
[[Category: Khoudian C]] | |||
[[Category: Lowe ED]] | |||
[[Category: Noble MEM]] | |||
[[Category: Paraskevopoulos K]] | |||
[[Category: Riedinger C]] | |||
[[Category: Smith D]] | |||
Latest revision as of 05:42, 21 November 2024
Crystal structure of S. pombe Rpn12Crystal structure of S. pombe Rpn12
Structural highlights
Publication Abstract from PubMedThe ubiquitin proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. We report the crystal structure of Rpn12, a proteasomal PCI- domain containing protein. The structure helps to define a core structural motif for the PCI-domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo. Structural and functional characterisation of Rpn12 identifies residues required for Rpn10 proteasome incorporation.,Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA Biochem J. 2012 Aug 20. PMID:22906049[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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