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| | <StructureSection load='1y6l' size='340' side='right'caption='[[1y6l]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='1y6l' size='340' side='right'caption='[[1y6l]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y6l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y6L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y6l]] is a 3 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=1Y6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y6L FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBE2E2, UBCH8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1y6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6l OCA], [https://pdbe.org/1y6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y6l RCSB], [https://www.ebi.ac.uk/pdbsum/1y6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6l ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6l OCA], [http://pdbe.org/1y6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y6l RCSB], [http://www.ebi.ac.uk/pdbsum/1y6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UB2E2_HUMAN UB2E2_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination.<ref>PMID:9371400</ref> <ref>PMID:20061386</ref> | + | [https://www.uniprot.org/uniprot/UB2E2_HUMAN UB2E2_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination.<ref>PMID:9371400</ref> <ref>PMID:20061386</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]] | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ubiquitin--protein ligase]]
| + | [[Category: Arrowsmith C]] |
| - | [[Category: Arrowsmith, C]] | + | [[Category: Avvakumov GV]] |
| - | [[Category: Avvakumov, G V]] | + | [[Category: Bochkarev A]] |
| - | [[Category: Bochkarev, A]] | + | [[Category: Dhe-Paganon S]] |
| - | [[Category: Dhe-Paganon, S]] | + | [[Category: Edwards A]] |
| - | [[Category: Edwards, A]] | + | [[Category: Kozieradzki I]] |
| - | [[Category: Kozieradzki, I]] | + | [[Category: Mackenzie F]] |
| - | [[Category: Mackenzie, F]] | + | [[Category: Newman EM]] |
| - | [[Category: Newman, E M]] | + | [[Category: Sundstrom M]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Walker JR]] |
| - | [[Category: Sundstrom, M]] | + | |
| - | [[Category: Walker, J R]] | + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| - | [[Category: Ubiquitin-conjugating enzyme]]
| + | |
| Structural highlights
Function
UB2E2_HUMAN Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kimura M, Hattori T, Matsuda Y, Yoshioka T, Sumi N, Umeda Y, Nakashima S, Okano Y. cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme. Cytogenet Cell Genet. 1997;78(2):107-11. PMID:9371400
- ↑ David Y, Ziv T, Admon A, Navon A. The E2 ubiquitin conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Jan 8. PMID:20061386 doi:M109.089003
- ↑ 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. A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Mol Cell Proteomics. 2012 Aug;11(8):329-41. Epub 2012 Apr 10. PMID:22496338 doi:http://dx.doi.org/10.1074/mcp.O111.013706
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