4b0z: Difference between revisions
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<StructureSection load='4b0z' size='340' side='right'caption='[[4b0z]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='4b0z' size='340' side='right'caption='[[4b0z]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b0z]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4b0z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SGM:MONOTHIOGLYCEROL'>SGM</scene></td></tr> | </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'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RPN12_SCHPO RPN12_SCHPO]] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Proteasome|Proteasome]] | *[[Proteasome 3D structures|Proteasome 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cbs 356]] | [[Category: Cbs 356]] | ||
[[Category: Large Structures]] | |||
[[Category: Boehringer, J]] | [[Category: Boehringer, J]] | ||
[[Category: Endicott, J A]] | [[Category: Endicott, J A]] | ||
Revision as of 08:53, 25 August 2022
Crystal structure of S. pombe Rpn12Crystal structure of S. pombe Rpn12
Structural highlights
Function[RPN12_SCHPO] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. 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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