2g3q: Difference between revisions

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-[[Image:2g3q.png|left|200px]]
-<!--
+==Solution Structure of Ede1 UBA-ubiquitin complex==
-The line below this paragraph, containing "STRUCTURE_2g3q", creates the "Structure Box" on the page.
+<StructureSection load='2g3q' size='340' side='right'caption='[[2g3q]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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'>[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>
-{{STRUCTURE_2g3q|  PDB=2g3q  |  SCENE=  }}
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=2g3q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Solution Structure of Ede1 UBA-ubiquitin complex===
+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<ref>PMID:16563434</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16563434}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2g3q" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16563434 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_16563434}}
-==About this Structure==
-[[2g3q]] is a 2 chain structure of [[Ubiquitin]] 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].
 ==See Also==
-*[[Ubiquitin]]
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:16563434</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Hicke, L.]]
+[[Category: Hicke L]]
-[[Category: Radhakrishnan, I.]]
+[[Category: Radhakrishnan I]]
-[[Category: Swanson, K A.]]
+[[Category: Swanson KA]]
-[[Category: Endocytosis]]
-[[Category: Endocytosis/signaling protein complex]]
-[[Category: Monoubiquitin signaling]]
-[[Category: Solution structure]]
-[[Category: Uba domain]]
-[[Category: Ubiquitin-binding motif]]