Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein

Changwen Jin, Tatanya Shiyanova, Zhiyuan Shen, Xiubei Liao

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The structure of a ubiquitin-like protein, small ubiquitin-related modifier-1 (SUMO-1), was earlier determined using homonuclear nuclear magnetic resonance (NMR) spectroscopy, since the spectral quality of the protein was not suitable for heteronuclear NMR data collection. In this study, a slightly different construct of the SUMO-1 gene was used for protein over-expression. The protein purified from this construct showed high spectral qualities, therefore, multi-dimensional heteronuclear NMR data for a dynamic study and structural determination were acquired. The structure of SUMO-1 obtained in this study differs in several respects from the structure obtained from homonuclear NMR data. Furthermore, structural differences were observed between the new SUMO-1 and ubiquitin structures. These differences may be important for SUMO-1-specific recognition in cells. Additionally, relaxation parameters indicate that SUMO-1 undergoes highly anisotropic tumbling in solution and that the long amino (N)-terminal sequence of SUMO-1 is highly dynamic with increasing flexibility towards the end.

Original languageEnglish (US)
Pages (from-to)227-234
Number of pages8
JournalInternational Journal of Biological Macromolecules
Volume28
Issue number3
DOIs
StatePublished - Mar 13 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

Keywords

  • Nuclear magnetic resonance
  • Protein structure and dynamics
  • SUMO-1
  • Ubiquitin-like protein

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