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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Acknowledgments
The authors are grateful to Prof. Jochen Balbach (University of Halle, Germany) for providing access to the 800 MHz NMR spectrometer. This work was supported by German Ministry for Research and Education Grants BMBF 0315638B and 03IS2211H.
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Lin, YJ., Schmidt, A., Burgardt, N.I. et al. 1H, 13C and 15N resonance assignments of human parvulin 17. Biomol NMR Assign 7, 325–329 (2013). https://doi.org/10.1007/s12104-012-9438-2
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DOI: https://doi.org/10.1007/s12104-012-9438-2