Solution structure of ThiS and implications for the evolutionary roots of ubiquitin

  title={Solution structure of ThiS and implications for the evolutionary roots of ubiquitin},
  author={Chunyu Wang and Jun Xi and Tadhg P. Begley and Linda K. Nicholson},
  journal={Nature Structural Biology},
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… 

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Structural analysis of Escherichia coli ThiF.

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Pathways of ubiquitin conjugation

  • A. HaasT. Siepmann
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1997
The covalent attachment of the polypeptide ubiquitin to proteins marks them for degradation by the ubiquitin/26S proteasome‐dependent degradation pathway. This pathway functions in regulating many

Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.

The covalent and non-covalent interaction sites are clearly separated on the HsUbc2b surface, while no such clear-cut segregation of the interaction area was observed on ubiquitin.

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Evolution and function of ubiquitin-like protein-conjugation systems

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Eukaryotic Molybdopterin Synthase

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Ubiquitin and its kin: how close are the family ties?