1f0z

<StructureSection load='1f0z' size='340' side='right'caption='[[1f0z]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1f0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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'>[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>

[[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>

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== 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<ref>PMID:11135670</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1f0z" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Begley, T P]]

[[Category: Nicholson, L K]]

[[Category: Wang, C]]

[[Category: Xi, J]]

[[Category: Ubiquitin fold]]