2r2y

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[[Image:2r2y.jpg|left|200px]]
 
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==Crystal structure of the proteasomal Rpn13 PRU-domain==
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The line below this paragraph, containing "STRUCTURE_2r2y", creates the "Structure Box" on the page.
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<StructureSection load='2r2y' size='340' side='right'caption='[[2r2y]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2r2y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R2Y FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=2r2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r2y OCA], [https://pdbe.org/2r2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r2y RCSB], [https://www.ebi.ac.uk/pdbsum/2r2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r2y ProSAT]</span></td></tr>
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{{STRUCTURE_2r2y| PDB=2r2y | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of the proteasomal Rpn13 PRU-domain'''
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r2/2r2y_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2R2Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R2Y OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r2y ConSurf].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18497827 18497827]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Dikic I]]
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[[Category: Dikic, I.]]
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[[Category: Finley D]]
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[[Category: Finley, D.]]
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[[Category: Groll M]]
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[[Category: Groll, M.]]
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[[Category: Walters K]]
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[[Category: Walters, K.]]
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[[Category: 19s regulator]]
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[[Category: Ph-domain]]
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[[Category: Proteasome]]
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[[Category: Protein binding]]
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[[Category: Receptor]]
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[[Category: Receptor domain for ubiquitin and proteasome binding]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitin-proteasome-degradation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:58:53 2008''
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Current revision

Crystal structure of the proteasomal Rpn13 PRU-domain

PDB ID 2r2y

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