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| ==Crystal structure of Tum1 protein from Saccharomyces cerevisiae== | | ==Crystal structure of Tum1 protein from Saccharomyces cerevisiae== |
- | <StructureSection load='3utn' size='340' side='right' caption='[[3utn]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3utn' size='340' side='right'caption='[[3utn]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3utn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3utn]] is a 1 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=3UTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTN FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TUM1, YOR251C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] </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=3utn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utn OCA], [https://pdbe.org/3utn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utn RCSB], [https://www.ebi.ac.uk/pdbsum/3utn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utn ProSAT]</span></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=3utn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utn OCA], [http://pdbe.org/3utn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3utn RCSB], [http://www.ebi.ac.uk/pdbsum/3utn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3utn ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/THTR_YEAST THTR_YEAST]] Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.<ref>PMID:18755837</ref> | + | [https://www.uniprot.org/uniprot/THTR_YEAST THTR_YEAST] Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.<ref>PMID:18755837</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
- | [[Category: Thiosulfate sulfurtransferase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
- | [[Category: Gong, W]] | + | [[Category: Gong W]] |
- | [[Category: Ji, C]] | + | [[Category: Ji C]] |
- | [[Category: Liu, M]] | + | [[Category: Liu M]] |
- | [[Category: Qiu, R]] | + | [[Category: Qiu R]] |
- | [[Category: Wang, F]] | + | [[Category: Wang F]] |
- | [[Category: Rhodanese-like domain]]
| + | |
- | [[Category: Sulfurtransferase]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Function
THTR_YEAST Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.[1]
Publication Abstract from PubMed
Yeast tRNA-thiouridine modification protein 1 (Tum1) plays essential role in the sulfur transfer process of Urm1 system, which in turn is involved in many important cellular processes. In the rhodanese-like domain (RLD), conserved cysteine residue is proved to be the centre of active site of sulfurtransferases and crucial for the substrate recognition. In this report, we describe the crystal structure of Tum1 protein at 1.90 A resolution which, despite consisting of two RLDs, has only one conserved cysteine residue in the C-terminal RLD. An unaccounted electron density is found near the active site, which might point to the new cofactor in the sulfur transfer mechanism.
Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae.,Qiu R, Wang F, Liu M, Lou T, Ji C Protein Pept Lett. 2012 May 8. PMID:22587783[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang B, Lu J, Bystrom AS. A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae. RNA. 2008 Oct;14(10):2183-94. doi: 10.1261/rna.1184108. Epub 2008 Aug 28. PMID:18755837 doi:10.1261/rna.1184108
- ↑ Qiu R, Wang F, Liu M, Lou T, Ji C. Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae. Protein Pept Lett. 2012 May 8. PMID:22587783
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