|
|
(7 intermediate revisions not shown.) |
Line 1: |
Line 1: |
- | [[Image:3k9p.png|left|200px]] | |
| | | |
- | <!--
| + | ==The crystal structure of E2-25K and ubiquitin complex== |
- | The line below this paragraph, containing "STRUCTURE_3k9p", creates the "Structure Box" on the page.
| + | <StructureSection load='3k9p' size='340' side='right'caption='[[3k9p]], [[Resolution|resolution]] 2.80Å' 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'>[[3k9p]] is a 2 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=3K9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K9P 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]] 2.8Å</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=3k9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k9p OCA], [https://pdbe.org/3k9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k9p RCSB], [https://www.ebi.ac.uk/pdbsum/3k9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k9p ProSAT]</span></td></tr> |
- | {{STRUCTURE_3k9p| PDB=3k9p | SCENE= }}
| + | </table> |
- | | + | == Function == |
- | ===The crystal structure of E2-25K and ubiquitin complex===
| + | [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> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_20826778}}, adds the Publication Abstract to the page
| + | <jmolCheckbox> |
- | (as it appears on PubMed at http://www.pubmed.gov), where 20826778 is the PubMed ID number.
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/3k9p_consurf.spt"</scriptWhenChecked> |
- | -->
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | {{ABSTRACT_PUBMED_20826778}}
| + | <text>to colour the structure by Evolutionary Conservation</text> |
- | | + | </jmolCheckbox> |
- | ==About this Structure== | + | </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=3k9p ConSurf]. |
- | [[3k9p]] is a 2 chain structure of [[Ubiquitin]] 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=3K9P OCA]. | + | <div style="clear:both"></div> |
| | | |
| ==See Also== | | ==See Also== |
- | *[[Ubiquitin]] | + | *[[Ubiquitin|Ubiquitin]] |
- | | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
- | ==Reference== | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
- | <ref group="xtra">PMID:20826778</ref><references group="xtra"/> | + | == References == |
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Ubiquitin--protein ligase]] | + | [[Category: Large Structures]] |
- | [[Category: Eom, S H.]] | + | [[Category: Eom SH]] |
- | [[Category: Kang, G B.]] | + | [[Category: Kang GB]] |
- | [[Category: Ko, S.]] | + | [[Category: Ko S]] |
- | [[Category: Lee, W.]] | + | [[Category: Lee W]] |
- | [[Category: Song, S M.]] | + | [[Category: Song SM]] |
- | [[Category: Atp-binding]]
| + | |
- | [[Category: Complex structure]]
| + | |
- | [[Category: E2-25k]]
| + | |
- | [[Category: Isopeptide bond]]
| + | |
- | [[Category: Ligase]]
| + | |
- | [[Category: Ligase-signaling protein complex]]
| + | |
- | [[Category: Nucleotide-binding]]
| + | |
- | [[Category: Nucleus]]
| + | |
- | [[Category: Phosphoprotein]]
| + | |
- | [[Category: Ubiquitin]]
| + | |
- | [[Category: Ubl conjugation pathway]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Kalchman MA, Graham RK, Xia G, Koide HB, Hodgson JG, Graham KC, Goldberg YP, Gietz RD, Pickart CM, Hayden MR. Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J Biol Chem. 1996 Aug 9;271(32):19385-94. PMID:8702625
- ↑ Kikuchi J, Furukawa Y, Kubo N, Tokura A, Hayashi N, Nakamura M, Matsuda M, Sakurabayashi I. Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for atherosclerosis. Arterioscler Thromb Vasc Biol. 2000 Jan;20(1):128-34. PMID:10634809
- ↑ Furukawa Y, Kubo N, Kikuchi J, Tokura A, Fujita N, Sakurabayashi I. Regulation of macrophage-specific gene expression by degenerated lipoproteins. Electrophoresis. 2000 Jan;21(2):338-46. PMID:10675012 doi:<338::AID-ELPS338>3.0.CO;2-9 http://dx.doi.org/10.1002/(SICI)1522-2683(20000101)21:2<338::AID-ELPS338>3.0.CO;2-9
- ↑ Yamada M, Ohnishi J, Ohkawara B, Iemura S, Satoh K, Hyodo-Miura J, Kawachi K, Natsume T, Shibuya H. NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF). J Biol Chem. 2006 Jul 28;281(30):20749-60. Epub 2006 May 19. PMID:16714285 doi:http://dx.doi.org/10.1074/jbc.M602089200
- ↑ Flierman D, Coleman CS, Pickart CM, Rapoport TA, Chau V. E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11589-94. Epub 2006 Jul 25. PMID:16868077 doi:http://dx.doi.org/0605215103
- ↑ Christensen DE, Brzovic PS, Klevit RE. E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages. Nat Struct Mol Biol. 2007 Oct;14(10):941-8. Epub 2007 Sep 16. PMID:17873885 doi:http://dx.doi.org/10.1038/nsmb1295
- ↑ 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
- ↑ Oh KJ, Kalinina A, Bagchi S. Destabilization of Rb by human papillomavirus E7 is cell cycle dependent: E2-25K is involved in the proteolysis. Virology. 2010 Jan 5;396(1):118-24. doi: 10.1016/j.virol.2009.10.018. Epub 2009, Nov 10. PMID:19906396 doi:http://dx.doi.org/10.1016/j.virol.2009.10.018
|