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1H, 13C and 15N resonance assignments of human parvulin 17 |
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| Authors: | Yi-Jan Lin Andreas Schmidt Noelia Inés Burgardt Alexandra Thiele Matthias Weiwad Christian Lücke |
| Affiliation: | 1. Graduate Institute of Natural Products and Center of Excellence for Environmental Medicine, Kaohsiung Medical University, Kaohsiung, 807, Taiwan 2. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle (Saale), Germany 3. Institute of Biochemistry and Biophysics (IQUIFIB), School of Pharmacy and Biochemistry, University of Buenos Aires, Junín 956, C1113AAD, Buenos Aires, Argentina |
| 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). |
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