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| | ==Solution Structure of Ede1 UBA-ubiquitin complex== | | ==Solution Structure of Ede1 UBA-ubiquitin complex== |
| - | <StructureSection load='2g3q' size='340' side='right' caption='[[2g3q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2g3q' size='340' side='right'caption='[[2g3q]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g3q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G3Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g3q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G3Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ede1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2g3q RCSB], [http://www.ebi.ac.uk/pdbsum/2g3q PDBsum]</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=2g3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3q OCA], [https://pdbe.org/2g3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g3q RCSB], [https://www.ebi.ac.uk/pdbsum/2g3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g3q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YBE7_YEAST YBE7_YEAST]] Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.<ref>PMID:10954428</ref> <ref>PMID:12529323</ref> <ref>PMID:16239147</ref> <ref>PMID:18448668</ref> <ref>PMID:22190733</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref> | + | [https://www.uniprot.org/uniprot/EDE1_YEAST EDE1_YEAST] Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.<ref>PMID:10954428</ref> <ref>PMID:12529323</ref> <ref>PMID:16239147</ref> <ref>PMID:18448668</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref> <ref>PMID:22190733</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/2g3q_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/2g3q_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| - | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </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=2g3q ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2g3q" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ubiquitin|Ubiquitin]] | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hicke, L]] | + | [[Category: Hicke L]] |
| - | [[Category: Radhakrishnan, I]] | + | [[Category: Radhakrishnan I]] |
| - | [[Category: Swanson, K A]] | + | [[Category: Swanson KA]] |
| - | [[Category: Endocytosis]]
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| - | [[Category: Endocytosis-signaling protein complex]]
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| - | [[Category: Monoubiquitin signaling]]
| + | |
| - | [[Category: Solution structure]]
| + | |
| - | [[Category: Uba domain]]
| + | |
| - | [[Category: Ubiquitin-binding motif]]
| + | |
| Structural highlights
Function
EDE1_YEAST Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.[1] [2] [3] [4] [5] [6] [7]
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
Monoubiquitination is a general mechanism for downregulating the activity of cell surface receptors by consigning these proteins for lysosome-mediated degradation through the endocytic pathway. The yeast Ede1 protein functions at the internalization step of endocytosis and binds monoubiquitinated proteins through a ubiquitin associated (UBA) domain. UBA domains are found in a broad range of cellular proteins but previous studies have suggested that the mode of ubiquitin recognition might not be universally conserved. Here we present the solution structure of the Ede1 UBA domain in complex with monoubiquitin. The Ede1 UBA domain forms a three-helix bundle structure and binds ubiquitin through a largely hydrophobic surface in a manner reminiscent of the Dsk2 UBA and the remotely homologous Cue2 CUE domains, for which high-resolution structures have been described. However, the interaction is dissimilar to the molecular models proposed for the hHR23A UBA domains bound to either monoubiquitin or Lys48-linked diubiquitin. Our mutational analyses of the Ede1 UBA domain-ubiquitin interaction reveal several key affinity determinants and, unexpectedly, a negative affinity determinant in the wild-type Ede1 protein, implying that high-affinity interactions may not be the sole criterion for optimal function of monoubiquitin-binding endocytic proteins.
Structural basis for monoubiquitin recognition by the Ede1 UBA domain.,Swanson KA, Hicke L, Radhakrishnan I J Mol Biol. 2006 May 5;358(3):713-24. Epub 2006 Mar 9. PMID:16563434[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gagny B, Wiederkehr A, Dumoulin P, Winsor B, Riezman H, Haguenauer-Tsapis R. A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis. J Cell Sci. 2000 Sep;113 ( Pt 18):3309-19. PMID:10954428
- ↑ Aguilar RC, Watson HA, Wendland B. The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J Biol Chem. 2003 Mar 21;278(12):10737-43. Epub 2003 Jan 14. PMID:12529323 doi:http://dx.doi.org/10.1074/jbc.M211622200
- ↑ Kaksonen M, Toret CP, Drubin DG. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell. 2005 Oct 21;123(2):305-20. PMID:16239147 doi:http://dx.doi.org/10.1016/j.cell.2005.09.024
- ↑ Maldonado-Baez L, Dores MR, Perkins EM, Drivas TG, Hicke L, Wendland B. Interaction between Epsin/Yap180 adaptors and the scaffolds Ede1/Pan1 is required for endocytosis. Mol Biol Cell. 2008 Jul;19(7):2936-48. Epub 2008 Apr 30. PMID:18448668 doi:http://dx.doi.org/E07-10-1019
- ↑ Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B. Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939 doi:10.1038/emboj.2009.248
- ↑ Stimpson HE, Toret CP, Cheng AT, Pauly BS, Drubin DG. Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol Biol Cell. 2009 Nov;20(22):4640-51. Epub 2009 Sep 23. PMID:19776351 doi:http://dx.doi.org/E09-05-0429
- ↑ Carroll SY, Stimpson HE, Weinberg J, Toret CP, Sun Y, Drubin DG. Analysis of yeast endocytic site formation and maturation through a regulatory transition point. Mol Biol Cell. 2012 Feb;23(4):657-68. doi: 10.1091/mbc.E11-02-0108. Epub 2011 Dec, 21. PMID:22190733 doi:http://dx.doi.org/10.1091/mbc.E11-02-0108
- ↑ Swanson KA, Hicke L, Radhakrishnan I. Structural basis for monoubiquitin recognition by the Ede1 UBA domain. J Mol Biol. 2006 May 5;358(3):713-24. Epub 2006 Mar 9. PMID:16563434 doi:10.1016/j.jmb.2006.02.059
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