Article

Biomolecular NMR Assignments

, Volume 7, Issue 2, pp 325-329

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

  • Yi-Jan LinAffiliated withGraduate Institute of Natural Products and Center of Excellence for Environmental Medicine, Kaohsiung Medical University
  • , Andreas SchmidtAffiliated withMax Planck Research Unit for Enzymology of Protein Folding
  • , Noelia Inés BurgardtAffiliated withMax Planck Research Unit for Enzymology of Protein FoldingInstitute of Biochemistry and Biophysics (IQUIFIB), School of Pharmacy and Biochemistry, University of Buenos Aires
  • , Alexandra ThieleAffiliated withMax Planck Research Unit for Enzymology of Protein Folding
  • , Matthias WeiwadAffiliated withMax Planck Research Unit for Enzymology of Protein Folding
  • , Christian LückeAffiliated withMax Planck Research Unit for Enzymology of Protein Folding Email author 

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

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