6if1
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of Ube2K and K48-linked di-ubiquitin complex== | |
+ | <StructureSection load='6if1' size='340' side='right'caption='[[6if1]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6if1]] 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=6IF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IF1 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]] 2.466Å</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=6if1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6if1 OCA], [https://pdbe.org/6if1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6if1 RCSB], [https://www.ebi.ac.uk/pdbsum/6if1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6if1 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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Ubiquitin-conjugating enzymes (E2) form thioester bonds with ubiquitin (Ub), which are subsequently transferred to target proteins for cellular progress. Ube2K/E2-25K (a class II E2 enzyme) contains a C-terminal ubiquitin-associated (UBA) domain that has been suggested to control ubiquitin recognition, dimerization, or poly-ubiquitin chain formation. Ube2K is a special E2 because it synthesizes K48-linked poly-ubiquitin chains without E3 ubiquitin ligase. We found that a novel interaction between the acceptor di-Ub (Ub(2)) and the auxiliary Ube2K promotes the discharging reaction and production of tri-Ub (Ub(3)), probably by guiding and positioning the K48 (in the distal Ub) of the acceptor Ub(2) in the active site. We also determined the crystal structure of Ube2K-Ub(2) at 2.47â¯A resolution. Based on our structural and biochemical data, we proposed a structural model of Ub(3) synthesis by Ube2K without E3. | ||
- | + | Crystal structure of the Ube2K/E2-25K and K48-linked di-ubiquitin complex provides structural insight into the mechanism of K48-specific ubiquitin chain synthesis.,Lee JG, Youn HS, Kang JY, Park SY, Kidera A, Yoo YJ, Eom SH Biochem Biophys Res Commun. 2018 Nov 17;506(1):102-107. doi: , 10.1016/j.bbrc.2018.10.067. Epub 2018 Oct 16. PMID:30336976<ref>PMID:30336976</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6if1" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
+ | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: An JY]] | ||
+ | [[Category: Eom SH]] | ||
+ | [[Category: Kang JY]] | ||
+ | [[Category: Lee J-G]] | ||
+ | [[Category: Lee Y]] | ||
+ | [[Category: Lim JJ]] | ||
+ | [[Category: Park KR]] | ||
+ | [[Category: Youn H-S]] |
Current revision
Crystal structure of Ube2K and K48-linked di-ubiquitin complex
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Categories: Homo sapiens | Large Structures | An JY | Eom SH | Kang JY | Lee J-G | Lee Y | Lim JJ | Park KR | Youn H-S