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| - | ==Not4 ring domain in complex Ubc4== | + | |
| - | <StructureSection load='5aie' size='340' side='right' caption='[[5aie]], [[Resolution|resolution]] 2.80Å' scene=''> | + | ==Not4 ring domain in complex with Ubc4== |
| | + | <StructureSection load='5aie' size='340' side='right'caption='[[5aie]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5aie]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AIE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5aie]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AIE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.8Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5aie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aie RCSB], [http://www.ebi.ac.uk/pdbsum/5aie PDBsum]</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=5aie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aie OCA], [https://pdbe.org/5aie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aie RCSB], [https://www.ebi.ac.uk/pdbsum/5aie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aie ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NOT4_YEAST NOT4_YEAST]] Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.<ref>PMID:9463387</ref> [[http://www.uniprot.org/uniprot/UBC4_YEAST UBC4_YEAST]] Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5.<ref>PMID:17550898</ref> | + | [https://www.uniprot.org/uniprot/NOT4_YEAST NOT4_YEAST] Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.<ref>PMID:9463387</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 5aie" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ubiquitin--protein ligase]] | + | [[Category: Large Structures]] |
| - | [[Category: Basquin, J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Bhaskar, V]] | + | [[Category: Basquin J]] |
| - | [[Category: Conti, E]] | + | [[Category: Bhaskar V]] |
| - | [[Category: E2-e3 ligase]] | + | [[Category: Conti E]] |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Not4 ring domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Ubc4]]
| + | |
| Structural highlights
Function
NOT4_YEAST Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.[1]
Publication Abstract from PubMed
The Ccr4-Not complex regulates eukaryotic gene expression at multiple levels, including mRNA turnover, translational repression, and transcription. We have studied the ubiquitylation module of the yeast Ccr4-Not complex and addressed how E3 ligase binds cognate E2 and how it is tethered to the complex. The 2.8-A resolution crystal structure of the N-terminal RING domain of Not4 in complex with Ubc4 shows the detailed interactions of this E3-E2 complex. The 3.6-A resolution crystal structure of the C-terminal domain of the yeast Not4 in complex with the C-terminal domain of Not1 reveals how a largely extended region at the C-terminus of Not4 wraps around a HEAT-repeat region of Not1. This C-terminal region of Not4 is only partly conserved in metazoans, rationalizing its weaker Not1-binding properties. The structural and biochemical data show how Not1 can incorporate both the ubiquitylation module and the Not2-Not3/5 module concomitantly in the Ccr4-Not complex.
Architecture of the ubiquitylation module of the yeast ccr4-not complex.,Bhaskar V, Basquin J, Conti E Structure. 2015 May 5;23(5):921-8. doi: 10.1016/j.str.2015.03.011. Epub 2015 Apr , 23. PMID:25914052[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu HY, Badarinarayana V, Audino DC, Rappsilber J, Mann M, Denis CL. The NOT proteins are part of the CCR4 transcriptional complex and affect gene expression both positively and negatively. EMBO J. 1998 Feb 16;17(4):1096-106. PMID:9463387 doi:http://dx.doi.org/10.1093/emboj/17.4.1096
- ↑ Bhaskar V, Basquin J, Conti E. Architecture of the ubiquitylation module of the yeast ccr4-not complex. Structure. 2015 May 5;23(5):921-8. doi: 10.1016/j.str.2015.03.011. Epub 2015 Apr , 23. PMID:25914052 doi:http://dx.doi.org/10.1016/j.str.2015.03.011
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