3f92

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[[Image:3f92.png|left|200px]]
 
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{{STRUCTURE_3f92| PDB=3f92 | SCENE= }}
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==Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5==
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<StructureSection load='3f92' size='340' side='right'caption='[[3f92]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3f92]] is a 1 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=3F92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F92 FirstGlance]. <br>
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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]] 2.23&#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>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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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=3f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f92 OCA], [https://pdbe.org/3f92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f92 RCSB], [https://www.ebi.ac.uk/pdbsum/3f92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f92 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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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/f9/3f92_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=3f92 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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The ubiquitin-conjugating enzyme E2-25K has been identified as a huntingtin (the key protein in Huntington's disease) interacting protein and has been shown to play a role in mediating the toxicity of Abeta, the principal protein involved in Alzheimer's disease pathogenesis. E2-25K is a dual-domain protein with an ubiquitin-associated (UBA) domain as well as a conserved ubiquitin-conjugating (UBC) domain which catalyzes the formation of a covalent bond between the C-terminal glycine of an ubiquitin molecule and the -amine of a lysine residue on the acceptor protein as part of the ubiquitin-proteasome pathway. The crystal structures of E2-25K M172A mutant protein at pH 6.5 and pH 8.5 were determined to 1.9 and 2.2 A resolution, respectively. Examination of the structures revealed domain-domain interactions between the UBC and UBA domains which have not previously been reported.
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===Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5===
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Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).,Wilson RC, Hughes RC, Flatt JW, Meehan EJ, Ng JD, Twigg PD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):440-4. Epub 2009 Apr 24. PMID:19407372<ref>PMID:19407372</ref>
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{{ABSTRACT_PUBMED_19407372}}
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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 3f92" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[3f92]] is a 1 chain structure with 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=3F92 OCA].
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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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==Reference==
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<references/>
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<ref group="xtra">PMID:019407372</ref><references group="xtra"/>
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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: Flatt, J W.]]
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[[Category: Flatt JW]]
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[[Category: Hughes, R C.]]
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[[Category: Hughes RC]]
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[[Category: Meehan, E J.]]
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[[Category: Meehan EJ]]
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[[Category: Ng, J D.]]
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[[Category: Ng JD]]
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[[Category: Twigg, P D.]]
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[[Category: Twigg PD]]
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[[Category: Wilson, R C.]]
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[[Category: Wilson RC]]
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[[Category: E2-25k]]
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[[Category: Hip-2]]
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[[Category: Huntington interacting]]
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[[Category: Huntington-interacting protein 2]]
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[[Category: Ligase]]
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[[Category: Ubiquitin carrier protein]]
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[[Category: Ubiquitin-conjugating]]
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[[Category: Ubiquitin-conjugating enzyme e2 k]]
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[[Category: Ubiquitin-protein ligase]]
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[[Category: Ubl conjugation pathway]]
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Current revision

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5

PDB ID 3f92

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