2bf8: Difference between revisions

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-{{Seed}}
-[[Image:2bf8.png|left|200px]]
-<!--
+==Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K==
-The line below this paragraph, containing "STRUCTURE_2bf8", creates the "Structure Box" on the page.
+<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution|resolution]] 2.30&Aring;' 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'>[[2bf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF8 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">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [https://pdbe.org/2bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 ProSAT]</span></td></tr>
-{{STRUCTURE_2bf8|  PDB=2bf8  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UBE2K_BOVIN UBE2K_BOVIN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53 (By similarity). Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1.[UniProtKB:P61086]<ref>PMID:9535861</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/bf/2bf8_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=2bf8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (PsiKXE), and functions only in the context of an alpha-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets.
-===CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K===
+SUMO modification of the ubiquitin-conjugating enzyme E2-25K.,Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Korner R, Olsen JV, Jentsch S, Melchior F, Sixma TK Nat Struct Mol Biol. 2005 Mar;12(3):264-9. Epub 2005 Feb 20. PMID:15723079<ref>PMID:15723079</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bf8" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15723079}}, adds the Publication Abstract to the page
+*[[SUMO 3D Structures|SUMO 3D Structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15723079 is the PubMed ID number.
+*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
--->
+== References ==
-{{ABSTRACT_PUBMED_15723079}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-BF8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA].
-==Reference==
-SUMO modification of the ubiquitin-conjugating enzyme E2-25K., Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Korner R, Olsen JV, Jentsch S, Melchior F, Sixma TK, Nat Struct Mol Biol. 2005 Mar;12(3):264-9. Epub 2005 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15723079 15723079]
 [[Category: Bos taurus]]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Ubiquitin--protein ligase]]
+[[Category: Jentsch S]]
-[[Category: Dijk, W J.Van.]]
+[[Category: Knipscheer P]]
-[[Category: Jentsch, S.]]
+[[Category: Korner R]]
-[[Category: Knipscheer, P.]]
+[[Category: Melchior F]]
-[[Category: Korner, R.]]
+[[Category: Oberhofer E]]
-[[Category: Melchior, F.]]
+[[Category: Pichler A]]
-[[Category: Oberhofer, E.]]
+[[Category: Sixma TK]]
-[[Category: Olsen, J Velgaard.]]
+[[Category: Van Dijk WJ]]
-[[Category: Pichler, A.]]
+[[Category: Velgaard Olsen J]]
-[[Category: SPINE, Structural Proteomics in Europe.]]
-[[Category: Sixma, T K.]]
-[[Category: E2 ubiquitin conjugating enzyme]]
-[[Category: E2-25k]]
-[[Category: Ligase]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-[[Category: Sumo]]
-[[Category: Sumo-target structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:39:41 2008''