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| | ==U-box domain of the E3 Ubiquitin Ligase E4B== | | ==U-box domain of the E3 Ubiquitin Ligase E4B== |
| - | <StructureSection load='2kr4' size='340' side='right' caption='[[2kr4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kr4' size='340' side='right'caption='[[2kr4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kr4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KR4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KR4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kr4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KR4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ube4b, Ufd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr4 OCA], [http://pdbe.org/2kr4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kr4 RCSB], [http://www.ebi.ac.uk/pdbsum/2kr4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kr4 ProSAT]</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=2kr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr4 OCA], [https://pdbe.org/2kr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kr4 RCSB], [https://www.ebi.ac.uk/pdbsum/2kr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kr4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UBE4B_MOUSE UBE4B_MOUSE]] Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity).<ref>PMID:11770485</ref> [UniProtKB:O95155] | + | [https://www.uniprot.org/uniprot/UBE4B_MOUSE UBE4B_MOUSE] Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity).<ref>PMID:11770485</ref> [UniProtKB:O95155] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Chazin, W]] | + | [[Category: Mus musculus]] |
| - | [[Category: Nordquist, K]] | + | [[Category: Chazin W]] |
| - | [[Category: Soss, S]] | + | [[Category: Nordquist K]] |
| - | [[Category: E3 ligase]] | + | [[Category: Soss S]] |
| - | [[Category: E4b]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Ring]]
| + | |
| - | [[Category: U-box]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| - | [[Category: Ubl conjugation pathway]]
| + | |
| - | [[Category: Ufd2]]
| + | |
| Structural highlights
Function
UBE4B_MOUSE Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity).[1] [UniProtKB:O95155]
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
Substantial evidence has accumulated indicating a significant role for oligomerization in the function of E3 ubiquitin ligases. Among the many characterized E3 ligases, the yeast U-box protein Ufd2 and its mammalian homologue E4B appear to be unique in functioning as monomers. An E4B U-box domain construct (E4BU) has been subcloned, overexpressed in Escherichia coli, and purified, which enabled determination of a high-resolution NMR solution structure and detailed biophysical analysis. E4BU is a stable monomeric protein that folds into the same structure observed for other structurally characterized U-box domain homodimers. Multiple sequence alignment combined with comparative structural analysis reveals substitutions in the sequence that inhibit dimerization. The interaction between E4BU and the E2 conjugating enzyme UbcH5c has been mapped using NMR, and these data have been used to generate a structural model for the complex. The E2 binding site is found to be similar to that observed for dimeric U-box and RING domain E3 ligases. Despite the inability to dimerize, E4BU was found to be active in a standard autoubiquitination assay. The structure of E4BU and its ability to function as a monomer are discussed in light of the ubiquitous observation of U-box and RING domain oligomerization.
Structural and functional characterization of the monomeric U-box domain from E4B.,Nordquist KA, Dimitrova YN, Brzovic PS, Ridenour WB, Munro KA, Soss SE, Caprioli RM, Klevit RE, Chazin WJ Biochemistry. 2010 Jan 19;49(2):347-55. PMID:20017557[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mack TG, Reiner M, Beirowski B, Mi W, Emanuelli M, Wagner D, Thomson D, Gillingwater T, Court F, Conforti L, Fernando FS, Tarlton A, Andressen C, Addicks K, Magni G, Ribchester RR, Perry VH, Coleman MP. Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene. Nat Neurosci. 2001 Dec;4(12):1199-206. PMID:11770485 doi:http://dx.doi.org/10.1038/nn770
- ↑ Nordquist KA, Dimitrova YN, Brzovic PS, Ridenour WB, Munro KA, Soss SE, Caprioli RM, Klevit RE, Chazin WJ. Structural and functional characterization of the monomeric U-box domain from E4B. Biochemistry. 2010 Jan 19;49(2):347-55. PMID:20017557 doi:10.1021/bi901620v
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