2bf8
From Proteopedia
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- | == | + | |
- | <StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution|resolution]] 2.30Å' scene=''> | + | ==Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K== |
+ | <StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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 == | == 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/bf/2bf8_consurf.spt"</scriptWhenChecked> | + | <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> | <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/ | + | </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="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 2bf8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
- | *[[SUMO|SUMO]] | + | *[[SUMO 3D Structures|SUMO 3D Structures]] |
- | *[[ | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | + | [[Category: Jentsch S]] | |
- | [[Category: Jentsch | + | [[Category: Knipscheer P]] |
- | [[Category: Knipscheer | + | [[Category: Korner R]] |
- | [[Category: Korner | + | [[Category: Melchior F]] |
- | [[Category: Melchior | + | [[Category: Oberhofer E]] |
- | [[Category: Oberhofer | + | [[Category: Pichler A]] |
- | + | [[Category: Sixma TK]] | |
- | [[Category: Pichler | + | [[Category: Van Dijk WJ]] |
- | [[Category: Sixma | + | [[Category: Velgaard Olsen J]] |
- | [[Category: | + | |
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Current revision
Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K
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