2o25: Difference between revisions

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New page: left|200px<br /> <applet load="2o25" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o25, resolution 2.60Å" /> '''Ubiquitin-Conjugati...
 
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[[Image:2o25.gif|left|200px]]<br />
<applet load="2o25" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2o25, resolution 2.60&Aring;" />
'''Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9'''<br />


==Disease==
==Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9==
Known disease associated with this structure: DNA ligase I deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=126391 126391]]
<StructureSection load='2o25' size='340' side='right'caption='[[2o25]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2o25]] is a 4 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=2O25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O25 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=2o25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o25 OCA], [https://pdbe.org/2o25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o25 RCSB], [https://www.ebi.ac.uk/pdbsum/2o25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o25 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBE2K_HUMAN UBE2K_HUMAN] 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. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.<ref>PMID:8702625</ref> <ref>PMID:10634809</ref> <ref>PMID:10675012</ref> <ref>PMID:16714285</ref> <ref>PMID:16868077</ref> <ref>PMID:17873885</ref> <ref>PMID:20061386</ref> <ref>PMID:19906396</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/o2/2o25_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=2o25 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2O25 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O25 OCA].
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C.H.]]
[[Category: Avvakumov GV]]
[[Category: Avvakumov, G.V.]]
[[Category: Bochkarev A]]
[[Category: Bochkarev, A.]]
[[Category: Dhe-Paganon S]]
[[Category: Dhe-Paganon, S.]]
[[Category: Edwards AM]]
[[Category: Edwards, A.M.]]
[[Category: Mackenzie F]]
[[Category: Mackenzie, F.]]
[[Category: Newman EM]]
[[Category: Newman, E.M.]]
[[Category: Sundstrom M]]
[[Category: SGC, Structural.Genomics.Consortium.]]
[[Category: Walker JR]]
[[Category: Sundstrom, M.]]
[[Category: Weigelt J]]
[[Category: Walker, J.R.]]
[[Category: Xue S]]
[[Category: Weigelt, J.]]
[[Category: Xue, S.]]
[[Category: ligase; ubl conjugation pathway]]
[[Category: sgc]]
[[Category: structural genomics consortium]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:05:29 2007''
Retrieved from "https://proteopedia.org/2o25"