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| | ==Solution Structure of Ubiquitin like protein from Mus Musculus== | | ==Solution Structure of Ubiquitin like protein from Mus Musculus== |
| - | <StructureSection load='1xo3' size='340' side='right'caption='[[1xo3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1xo3' size='340' side='right'caption='[[1xo3]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xo3]] 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=1XO3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XO3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xo3]] 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=1XO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XO3 FirstGlance]. <br> |
| - | </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=1xo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo3 OCA], [http://pdbe.org/1xo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xo3 RCSB], [http://www.ebi.ac.uk/pdbsum/1xo3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xo3 ProSAT], [http://www.topsan.org/Proteins/CESG/1xo3 TOPSAN]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=1xo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo3 OCA], [https://pdbe.org/1xo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xo3 RCSB], [https://www.ebi.ac.uk/pdbsum/1xo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xo3 ProSAT], [https://www.topsan.org/Proteins/CESG/1xo3 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/URM1_MOUSE URM1_MOUSE]] Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. May also act as an ubiquitin-like protein that is covalently conjugated to other proteins; the relevance of such function is however unclear in vivo (By similarity). | + | [https://www.uniprot.org/uniprot/URM1_MOUSE URM1_MOUSE] Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. May also act as an ubiquitin-like protein that is covalently conjugated to other proteins; the relevance of such function is however unclear in vivo (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Bahrami, A]] | + | [[Category: Bahrami A]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Lee MS]] |
| - | [[Category: Lee, M S]] | + | [[Category: Markley JL]] |
| - | [[Category: Markley, J L]] | + | [[Category: Singh S]] |
| - | [[Category: Singh, S]] | + | [[Category: Tonelli M]] |
| - | [[Category: Tonelli, M]] | + | [[Category: Tyler RC]] |
| - | [[Category: Tyler, R C]] | + | |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Unknown function]]
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| Structural highlights
Function
URM1_MOUSE Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. May also act as an ubiquitin-like protein that is covalently conjugated to other proteins; the relevance of such function is however unclear in vivo (By similarity).
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
We have used NMR spectroscopy to determine the solution structure of protein AAH26994.1 from Mus musculus and propose that it represents the first three-dimensional structure of a ubiquitin-related modifier 1 (Urm1) protein. Amino acid sequence comparisons indicate that AAH26994.1 belongs to the Urm1 family of ubiquitin-like modifier proteins. The best characterized member of this family has been shown to be involved in nutrient sensing, invasive growth, and budding in yeast. Proteins in this family have only a weak sequence similarity to ubiquitin, and the structure of AAH26994.1 showed a much closer resemblance to MoaD subunits of molybdopterin synthases (known structures are of three bacterial MoaD proteins with 14%-26% sequence identity to AAH26994.1). The structures of AAH26994.1 and the MoaD proteins each contain the signature ubiquitin secondary structure fold, but all differ from ubiquitin largely in regions outside of this fold. This structural similarity bolsters the hypothesis that ubiquitin and ubiquitin-related proteins evolved from a protein-based sulfide donor system of the molybdopterin synthase type.
Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1.,Singh S, Tonelli M, Tyler RC, Bahrami A, Lee MS, Markley JL Protein Sci. 2005 Aug;14(8):2095-102. PMID:16046629[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh S, Tonelli M, Tyler RC, Bahrami A, Lee MS, Markley JL. Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1. Protein Sci. 2005 Aug;14(8):2095-102. PMID:16046629 doi:14/8/2095
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