1xo3

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{{Seed}}
 
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[[Image:1xo3.png|left|200px]]
 
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==Solution Structure of Ubiquitin like protein from Mus Musculus==
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The line below this paragraph, containing "STRUCTURE_1xo3", creates the "Structure Box" on the page.
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<StructureSection load='1xo3' size='340' side='right'caption='[[1xo3]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_1xo3| PDB=1xo3 | SCENE= }}
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xo/1xo3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xo3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Solution Structure of Ubiquitin like protein from Mus Musculus===
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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<ref>PMID:16046629</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16046629}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1xo3" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16046629 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16046629}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1XO3 is a 1 chain structure of sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:16046629</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Bahrami, A.]]
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[[Category: Bahrami A]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Lee MS]]
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[[Category: Lee, M S.]]
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[[Category: Markley JL]]
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[[Category: Markley, J L.]]
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[[Category: Singh S]]
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[[Category: Singh, S.]]
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[[Category: Tonelli M]]
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[[Category: Tonelli, M.]]
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[[Category: Tyler RC]]
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[[Category: Tyler, R C.]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: Cesg]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: Unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:51:18 2009''
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Current revision

Solution Structure of Ubiquitin like protein from Mus Musculus

PDB ID 1xo3

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OCA

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