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| | ==SOLUTION STRUCTURE OF THIS, THE SULFUR CARRIER PROTEIN IN E.COLI THIAMIN BIOSYNTHESIS== | | ==SOLUTION STRUCTURE OF THIS, THE SULFUR CARRIER PROTEIN IN E.COLI THIAMIN BIOSYNTHESIS== |
| - | <StructureSection load='1f0z' size='340' side='right'caption='[[1f0z]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | + | <StructureSection load='1f0z' size='340' side='right'caption='[[1f0z]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f0z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F0Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0Z 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=1f0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0z OCA], [http://pdbe.org/1f0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f0z RCSB], [http://www.ebi.ac.uk/pdbsum/1f0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0z ProSAT]</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=1f0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0z OCA], [https://pdbe.org/1f0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0z RCSB], [https://www.ebi.ac.uk/pdbsum/1f0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THIS_ECOLI THIS_ECOLI]] Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.<ref>PMID:9632726</ref> | + | [https://www.uniprot.org/uniprot/THIS_ECOLI THIS_ECOLI] Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.<ref>PMID:9632726</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Begley, T P]] | + | [[Category: Begley TP]] |
| - | [[Category: Nicholson, L K]] | + | [[Category: Nicholson LK]] |
| - | [[Category: Wang, C]] | + | [[Category: Wang C]] |
| - | [[Category: Xi, J]] | + | [[Category: Xi J]] |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Ubiquitin fold]]
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| Structural highlights
Function
THIS_ECOLI Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.[1]
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
ThiS is a sulfur carrier protein that plays a central role in thiamin biosynthesis in Escherichia coli. Here we report the solution NMR structure of ThiS, the first for this class of sulfur carrier proteins. Although ThiS shares only 14% sequence identity with ubiquitin, it possesses the ubiquitin fold. This structural homology, combined with established functional similarities involving sulfur chemistry, demonstrates that the eukaryotic ubiquitin and the prokaryotic ThiS evolved from a common ancestor. This illustrates how structure determination is essential in establishing evolutionary links between proteins in which structure and function have been conserved through eons of evolution despite loss of sequence identity. The ThiS structure reveals both hydrophobic and electrostatic surface features that are likely determinants for interactions with binding partners. Comparison with surface features of ubiquitin and ubiquitin homologs SUMO-1, RUB-1 and NEDD8 suggest how Nature has utilized this single fold to incorporate similar chemistry into a broad array of highly specific biological processes.
Solution structure of ThiS and implications for the evolutionary roots of ubiquitin.,Wang C, Xi J, Begley TP, Nicholson LK Nat Struct Biol. 2001 Jan;8(1):47-51. PMID:11135670[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taylor SV, Kelleher NL, Kinsland C, Chiu HJ, Costello CA, Backstrom AD, McLafferty FW, Begley TP. Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J Biol Chem. 1998 Jun 26;273(26):16555-60. PMID:9632726
- ↑ Wang C, Xi J, Begley TP, Nicholson LK. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat Struct Biol. 2001 Jan;8(1):47-51. PMID:11135670 doi:10.1038/83041
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