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| | <StructureSection load='3odt' size='340' side='right'caption='[[3odt]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='3odt' size='340' side='right'caption='[[3odt]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3odt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ODT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3odt]] 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=3ODT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DOA1, UFD3, ZZZ4, YKL213C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3odt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odt OCA], [https://pdbe.org/3odt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odt RCSB], [https://www.ebi.ac.uk/pdbsum/3odt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odt 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=3odt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odt OCA], [https://pdbe.org/3odt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odt RCSB], [https://www.ebi.ac.uk/pdbsum/3odt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DOA1_YEAST DOA1_YEAST]] Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.<ref>PMID:15096053</ref> <ref>PMID:8890162</ref>
| + | [https://www.uniprot.org/uniprot/DOA1_YEAST DOA1_YEAST] Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.<ref>PMID:15096053</ref> <ref>PMID:8890162</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gakhar, L]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Pashkova, N]] | + | [[Category: Gakhar L]] |
| - | [[Category: Piper, R C]] | + | [[Category: Pashkova N]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Piper RC]] |
| - | [[Category: Winistorfer, S C]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Yu, L]] | + | [[Category: Winistorfer SC]] |
| - | [[Category: Nuclear protein]]
| + | [[Category: Yu L]] |
| - | [[Category: Ubiquitin]]
| + | |
| Structural highlights
Function
DOA1_YEAST Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.[1] [2]
Publication Abstract from PubMed
WD40-repeat beta-propellers are found in a wide range of proteins involved in distinct biological activities. We define a large subset of WD40 beta-propellers as a class of ubiquitin-binding domains. Using the beta-propeller from Doa1/Ufd3 as a paradigm, we find the conserved top surface of the Doa1 beta-propeller binds the hydrophobic patch of ubiquitin centered on residues I44, L8, and V70. Mutations that disrupt ubiquitin binding abrogate Doa1 function, demonstrating the importance of this interaction. We further demonstrate that WD40 beta-propellers from a functionally diverse set of proteins bind ubiquitin in a similar fashion. This set includes members of the F box family of SCF ubiquitin E3 ligase adaptors. Using mutants defective in binding, we find that ubiquitin interaction by the F box protein Cdc4 promotes its autoubiquitination and turnover. Collectively, our results reveal a molecular mechanism that may account for how ubiquitin controls a broad spectrum of cellular activities.
WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.,Pashkova N, Gakhar L, Winistorfer SC, Yu L, Ramaswamy S, Piper RC Mol Cell. 2010 Nov 12;40(3):433-43. PMID:21070969[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Russell NS, Wilkinson KD. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues. Biochemistry. 2004 Apr 27;43(16):4844-54. PMID:15096053 doi:10.1021/bi035626r
- ↑ Ghislain M, Dohmen RJ, Levy F, Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 1996 Sep 16;15(18):4884-99. PMID:8890162
- ↑ Pashkova N, Gakhar L, Winistorfer SC, Yu L, Ramaswamy S, Piper RC. WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol Cell. 2010 Nov 12;40(3):433-43. PMID:21070969 doi:10.1016/j.molcel.2010.10.018
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