2f4w

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[[Image:2f4w.gif|left|200px]]
 
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{{Structure
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==Human ubiquitin-conjugating enzyme E2 J2==
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|PDB= 2f4w |SIZE=350|CAPTION= <scene name='initialview01'>2f4w</scene>, resolution 2.00&Aring;
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<StructureSection load='2f4w' size='340' side='right'caption='[[2f4w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2f4w]] 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=2F4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F4W FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span>
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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]] 2&#8491;</td></tr>
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|GENE= UBE2J2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=2f4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f4w OCA], [https://pdbe.org/2f4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f4w RCSB], [https://www.ebi.ac.uk/pdbsum/2f4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f4w ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f4w OCA], [http://www.ebi.ac.uk/pdbsum/2f4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f4w RCSB]</span>
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[https://www.uniprot.org/uniprot/UB2J2_HUMAN UB2J2_HUMAN] Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).[PROSITE-ProRule:PRU00388]
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}}
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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/f4/2f4w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2f4w 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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'''Human ubiquitin-conjugating enzyme E2 J2'''
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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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</div>
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<div class="pdbe-citations 2f4w" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Degradation of proteins from the endoplasmic reticulum is fundamental to quality control within the secretory pathway, serves as a way of regulating levels of crucial proteins, and is utilized by viruses to enhance pathogenesis. In yeast two ubiquitin-conjugating enzymes (E2s), UBC6p and UBC7p are implicated in this process. We now report the characterization of murine homologs of these E2s. MmUBC6 is an integral membrane protein that is anchored via its hydrophobic C-terminal tail to the endoplasmic reticulum. MmUBC7, which is not an integral membrane protein, shows significant endoplasmic reticulum colocalization with MmUBC6. Overexpression of catalytically inactive MmUBC7 significantly delayed degradation from the endoplasmic reticulum of two T cell antigen receptor subunits, alpha and CD3-delta, and suggests a role for the ubiquitin conjugating system at the initiation of retrograde movement from the endoplasmic reticulum. These findings also implicate, for the first time, a specific E2 in degradation from the endoplasmic reticulum in mammalian cells.
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*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
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== References ==
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==About this Structure==
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<references/>
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2F4W is a [[Single protein]] structure of sequence 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=2F4W OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)., Tiwari S, Weissman AM, J Biol Chem. 2001 May 11;276(19):16193-200. Epub 2001 Feb 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11278356 11278356]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Arrowsmith C]]
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[[Category: Arrowsmith, C.]]
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[[Category: Avvakumov GV]]
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[[Category: Avvakumov, G V.]]
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[[Category: Bochkarev A]]
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[[Category: Bochkarev, A.]]
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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: Finerty Jr PJ]]
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[[Category: Jr., P J.Finerty.]]
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[[Category: Mackenzie F]]
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[[Category: Mackenzie, F.]]
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[[Category: Newman EM]]
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[[Category: Newman, E M.]]
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[[Category: Sundstrom M]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Walker JR]]
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[[Category: Sundstrom, M.]]
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[[Category: Weigelt J]]
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[[Category: Walker, J R.]]
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[[Category: Xue S]]
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[[Category: Weigelt, J.]]
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[[Category: Xue, S.]]
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[[Category: endoplasmic reticulum]]
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[[Category: ligase]]
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[[Category: structural genomics consortium (sgc)]]
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[[Category: ubl conjugation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:56 2008''
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Current revision

Human ubiquitin-conjugating enzyme E2 J2

PDB ID 2f4w

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