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| | ==Complex Structures of Mouse Rpn13 (22-130aa) and ubiquitin== | | ==Complex Structures of Mouse Rpn13 (22-130aa) and ubiquitin== |
| - | <StructureSection load='2z59' size='340' side='right'caption='[[2z59]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2z59' size='340' side='right'caption='[[2z59]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z59 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z59 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d3z|1d3z]], [[2hth|2hth]], [[2r2y|2r2y]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Adrm1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Rps27a, Uba80, Ubcep1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z59 OCA], [https://pdbe.org/2z59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z59 RCSB], [https://www.ebi.ac.uk/pdbsum/2z59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z59 ProSAT]</span></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=2z59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z59 OCA], [https://pdbe.org/2z59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z59 RCSB], [https://www.ebi.ac.uk/pdbsum/2z59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z59 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ADRM1_MOUSE ADRM1_MOUSE]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:15819879</ref> <ref>PMID:18497827</ref>
| + | [https://www.uniprot.org/uniprot/ADRM1_MOUSE ADRM1_MOUSE] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:15819879</ref> <ref>PMID:18497827</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chen, X]] | + | [[Category: Chen X]] |
| - | [[Category: Groll, M]] | + | [[Category: Groll M]] |
| - | [[Category: Schreiner, P]] | + | [[Category: Schreiner P]] |
| - | [[Category: Walters, K J]] | + | [[Category: Walters KJ]] |
| - | [[Category: Ph domain]]
| + | |
| - | [[Category: Proteasome]]
| + | |
| - | [[Category: Protein transport]]
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| Structural highlights
Function
ADRM1_MOUSE Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Targeted protein degradation is largely performed by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. It is currently unclear how the proteasome recognizes its substrates, as the only established ubiquitin receptor intrinsic to the proteasome is Rpn10/S5a (ref. 1), which is not essential for ubiquitin-mediated protein degradation in budding yeast. In the accompanying manuscript we report that Rpn13 (refs 3-7), a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 (refs 4-6) to the proteasome. Here we merge crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13. We determine the structure of Rpn13 alone and complexed with ubiquitin. The co-complex reveals a novel ubiquitin-binding mode in which loops rather than secondary structural elements are used to capture ubiquitin. Further support for the role of Rpn13 as a proteasomal ubiquitin receptor is demonstrated by its ability to bind ubiquitin and proteasome subunit Rpn2/S1 simultaneously. Finally, we provide a model structure of Rpn13 complexed to diubiquitin, which provides insights into how Rpn13 as a ubiquitin receptor is coupled to substrate deubiquitination by Uch37.
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.,Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M Nature. 2008 May 22;453(7194):548-52. PMID:18497827[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lamerant N, Kieda C. Adhesion properties of adhesion-regulating molecule 1 protein on endothelial cells. FEBS J. 2005 Apr;272(8):1833-44. PMID:15819879 doi:10.1111/j.1742-4658.2005.04613.x
- ↑ Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 2008 May 22;453(7194):548-52. PMID:18497827 doi:10.1038/nature06924
- ↑ Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 2008 May 22;453(7194):548-52. PMID:18497827 doi:10.1038/nature06924
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