1zuo

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{{Seed}}
 
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[[Image:1zuo.png|left|200px]]
 
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==Structure of Human Ubiquitin-Conjugating Enzyme (UBCi) Involved in Embryo Attachment and Implantation==
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The line below this paragraph, containing "STRUCTURE_1zuo", creates the "Structure Box" on the page.
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<StructureSection load='1zuo' size='340' side='right'caption='[[1zuo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1zuo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
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{{STRUCTURE_1zuo| PDB=1zuo | SCENE= }}
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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=1zuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuo OCA], [https://pdbe.org/1zuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zuo RCSB], [https://www.ebi.ac.uk/pdbsum/1zuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zuo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UB2Q2_HUMAN UB2Q2_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination.<ref>PMID:20061386</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zuo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1zuo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Here we describe a systematic structure-function analysis of the human ubiquitin (Ub) E2 conjugating proteins, consisting of the determination of 15 new high-resolution three-dimensional structures of E2 catalytic domains, and autoubiquitylation assays for 26 Ub-loading E2s screened against a panel of nine different HECT (homologous to E6-AP carboxyl terminus) E3 ligase domains. Integration of our structural and biochemical data revealed several E2 surface properties associated with Ub chain building activity; (1) net positive or neutral E2 charge, (2) an "acidic trough" located near the catalytic Cys, surrounded by an extensive basic region, and (3) similarity to the previously described HECT binding signature in UBE2L3 (UbcH7). Mass spectrometry was used to characterize the autoubiquitylation products of a number of functional E2-HECT pairs, and demonstrated that HECT domains from different subfamilies catalyze the formation of very different types of Ub chains, largely independent of the E2 in the reaction. Our data set represents the first comprehensive analysis of E2-HECT E3 interactions, and thus provides a framework for better understanding the molecular mechanisms of ubiquitylation.
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===Structure of Human Ubiquitin-Conjugating Enzyme (UBCi) Involved in Embryo Attachment and Implantation===
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A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen.,Sheng Y, Hong JH, Doherty R, Srikumar T, Shloush J, Avvakumov GV, Walker JR, Xue S, Neculai D, Wan JW, Kim SK, Arrowsmith CH, Raught B, Dhe-Paganon S Mol Cell Proteomics. 2012 Aug;11(8):329-41. Epub 2012 Apr 10. PMID:22496338<ref>PMID:22496338</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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1ZUO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUO OCA].
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<div class="pdbe-citations 1zuo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith C]]
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[[Category: Avvakumov, G V.]]
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[[Category: Avvakumov GV]]
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[[Category: Bochkarev, A.]]
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[[Category: Bochkarev A]]
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[[Category: Cui, H.]]
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[[Category: Cui H]]
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[[Category: Dhe-Paganon, S.]]
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[[Category: Dhe-Paganon S]]
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[[Category: Edwards, A.]]
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[[Category: Edwards A]]
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[[Category: Mackenzie, F.]]
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[[Category: Mackenzie F]]
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[[Category: Newman, E M.]]
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[[Category: Newman EM]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M.]]
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[[Category: Walker JR]]
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[[Category: Walker, J R.]]
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[[Category: Ligase]]
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[[Category: Structural genomics consortium ,sgc]]
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[[Category: Ubiquitin-conjugating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:52:48 2009''
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Current revision

Structure of Human Ubiquitin-Conjugating Enzyme (UBCi) Involved in Embryo Attachment and Implantation

PDB ID 1zuo

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