Biomolecular NMR Assignments

, Volume 7, Issue 2, pp 325–329

1H, 13C and 15N resonance assignments of human parvulin 17

Authors

  • Yi-Jan Lin
    • Graduate Institute of Natural Products and Center of Excellence for Environmental MedicineKaohsiung Medical University
  • Andreas Schmidt
    • Max Planck Research Unit for Enzymology of Protein Folding
  • Noelia Inés Burgardt
    • Max Planck Research Unit for Enzymology of Protein Folding
    • Institute of Biochemistry and Biophysics (IQUIFIB), School of Pharmacy and BiochemistryUniversity of Buenos Aires
  • Alexandra Thiele
    • Max Planck Research Unit for Enzymology of Protein Folding
  • Matthias Weiwad
    • Max Planck Research Unit for Enzymology of Protein Folding
    • Max Planck Research Unit for Enzymology of Protein Folding
Article

DOI: 10.1007/s12104-012-9438-2

Cite this article as:
Lin, Y., Schmidt, A., Burgardt, N.I. et al. Biomol NMR Assign (2013) 7: 325. doi:10.1007/s12104-012-9438-2

Abstract

A 25-residue elongation at the N-terminus endows parvulin 17 (Par17) with altered functional properties compared to parvulin 14 (Par14), such as an enhanced influence on microtubule assembly. Therefore the three-dimensional structure of this N-terminal elongation is of particular interest. Here, we report the nearly complete 1H, 13C and 15N chemical shift assignments of Par17. Subsequent chemical shift index analysis indicated that Par17 features a parvulin-type PPIase domain at the C-terminus, analogous to Par14, and an unstructured N-terminus encompassing the first 60 residues. Hence the N-terminus of Par17 apparently adopts a functionally-relevant structure only in presence of the respective interaction partner(s).

Keywords

PPIase Par14 Par17 DNA binding Microtubule assembly

Copyright information

© Springer Science+Business Media Dordrecht 2012