Pnc1 converts nicotinamide to nicotinic acid to generate NAD+ through the Preiss-Handler pathway that is one of the NAD+-salvage pathway. By reducing levels of nicotinamide, an inhibitor of the NAD+-dependent histone deacetylase Sir2, yeast Pnc1 contributes gene silencing. In this study, to understand the structural features and molecular mechanism of nicotinamidase Pnc1, we overexpressed, purified, and crystallized the N-terminally His6-tagged Pnc1 protein from Kluyveromyces lactis and obtained X-ray diffraction data at a resolution of 2.2 Å. The crystals of the K. lactis Pnc1 (KlPnc1) belonged to space group P212121 with unit cell parameters a=38.5, b=77.3, c=83.3, and α=β=γ= 90°. There is one molecule in the asymmetric unit.
We would like to thank beamline staff Yeon-Gil Kim at beamline 5C of the Pohang Accelerator Laboratory (Pohang, Korea) for data collection. This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science and ICT to JHC (2016R1C1B2009691).