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| | ==Structure of the conserved yeast listerin (Ltn1) N-terminal domain, MONOCLINIC FORM== | | ==Structure of the conserved yeast listerin (Ltn1) N-terminal domain, MONOCLINIC FORM== |
| - | <StructureSection load='5fg0' size='340' side='right' caption='[[5fg0]], [[Resolution|resolution]] 2.41Å' scene=''> | + | <StructureSection load='5fg0' size='340' side='right'caption='[[5fg0]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fg0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fg0]] 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=5FG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FG0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.41Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fg1|5fg1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=5fg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fg0 OCA], [http://pdbe.org/5fg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fg0 RCSB], [http://www.ebi.ac.uk/pdbsum/5fg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fg0 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=5fg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fg0 OCA], [https://pdbe.org/5fg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fg0 RCSB], [https://www.ebi.ac.uk/pdbsum/5fg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fg0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LTN1_YEAST LTN1_YEAST]] E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123). Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non-stop proteins) and other translation arrest products induced by poly-lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product (PubMed:20835226, PubMed:23825054, PubMed:24261871). May indirectly play a role in chromatin function and transcription (PubMed:17283062).<ref>PMID:17283062</ref> <ref>PMID:20835226</ref> <ref>PMID:23178123</ref> <ref>PMID:23825054</ref> <ref>PMID:24261871</ref> | + | [https://www.uniprot.org/uniprot/LTN1_YEAST LTN1_YEAST] E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123). Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non-stop proteins) and other translation arrest products induced by poly-lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product (PubMed:20835226, PubMed:23825054, PubMed:24261871). May indirectly play a role in chromatin function and transcription (PubMed:17283062).<ref>PMID:17283062</ref> <ref>PMID:20835226</ref> <ref>PMID:23178123</ref> <ref>PMID:23825054</ref> <ref>PMID:24261871</ref> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Doamekpor, S K]] | + | [[Category: Large Structures]] |
| - | [[Category: Lima, C D]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Ligase]] | + | [[Category: Doamekpor SK]] |
| - | [[Category: Protein quality control]] | + | [[Category: Lima CD]] |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ubiquitin ligase]]
| + | |
| Structural highlights
Function
LTN1_YEAST E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23178123). Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non-stop proteins) and other translation arrest products induced by poly-lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product (PubMed:20835226, PubMed:23825054, PubMed:24261871). May indirectly play a role in chromatin function and transcription (PubMed:17283062).[1] [2] [3] [4] [5]
See Also
References
- ↑ Braun MA, Costa PJ, Crisucci EM, Arndt KM. Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae. Mol Cell Biol. 2007 Apr;27(8):2800-11. Epub 2007 Feb 5. PMID:17283062 doi:http://dx.doi.org/10.1128/MCB.01947-06
- ↑ Bengtson MH, Joazeiro CA. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature. 2010 Sep 23;467(7314):470-3. doi: 10.1038/nature09371. Epub 2010 Sep 12. PMID:20835226 doi:http://dx.doi.org/10.1038/nature09371
- ↑ Brandman O, Stewart-Ornstein J, Wong D, Larson A, Williams CC, Li GW, Zhou S, King D, Shen PS, Weibezahn J, Dunn JG, Rouskin S, Inada T, Frost A, Weissman JS. A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress. Cell. 2012 Nov 21;151(5):1042-54. doi: 10.1016/j.cell.2012.10.044. PMID:23178123 doi:http://dx.doi.org/10.1016/j.cell.2012.10.044
- ↑ Letzring DP, Wolf AS, Brule CE, Grayhack EJ. Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1. RNA. 2013 Sep;19(9):1208-17. doi: 10.1261/rna.039446.113. Epub 2013 Jul 3. PMID:23825054 doi:http://dx.doi.org/10.1261/rna.039446.113
- ↑ Matsuda R, Ikeuchi K, Nomura S, Inada T. Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast. Genes Cells. 2014 Jan;19(1):1-12. doi: 10.1111/gtc.12106. Epub 2013 Nov 21. PMID:24261871 doi:http://dx.doi.org/10.1111/gtc.12106
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