Literature DB >> 30058168

Solution structure of a ubiquitin-like protein from Trypanosoma brucei.

Juan Mi1, Jiahai Zhang1, Shanhui Liao1, Xiaoming Tu1.   

Abstract

Ubiquitin-like proteins, similar to ubiquitin, can either exist freely or be covalently attached to other proteins via an enzymatic cascade. The ubiquitin-like proteins play roles in multiple biological processes including transcription, stress responses, DNA repair and so on. In this study, a novel ubiquitin-like protein (TbUbl11) was identified in Trypanosoma brucei. The solution structure of TbUbl11 was solved by NMR spectroscopy. TbUbl11 adopts a conserved β-grasp fold composed by a five-stranded β-sheet curling around a central α-helix, similar to other ubiquitin-like proteins. Meanwhile, some differences between TbUbl11 and other ubiquitin-like proteins were also identified. Additionally, we revealed that TbUbl11 is located in the whole cell body of procyclic-form T. brucei.
© 2018 The Protein Society.

Entities:  

Keywords:  NMR; Trypanosoma brucei; solution structure; ubiquitin-like protein

Mesh:

Substances:

Year:  2018        PMID: 30058168      PMCID: PMC6199154          DOI: 10.1002/pro.3492

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  22 in total

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Journal:  J Mol Biol       Date:  2002-05-24       Impact factor: 5.469

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Journal:  Biochim Biophys Acta       Date:  2004-11-29

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Authors:  Qiang Shang; Chao Xu; Jiahai Zhang; Xuecheng Zhang; Xiaoming Tu
Journal:  Proteins       Date:  2009-07

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Authors:  Rebecca L Welchman; Colin Gordon; R John Mayer
Journal:  Nat Rev Mol Cell Biol       Date:  2005-08       Impact factor: 94.444

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Review 10.  Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets.

Authors:  Lynn Bedford; James Lowe; Lawrence R Dick; R John Mayer; James E Brownell
Journal:  Nat Rev Drug Discov       Date:  2010-12-10       Impact factor: 84.694

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