지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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Pnc1 converts nicotinamide to nicotinic acid to generate NAD+ through the Preiss-Handler pathway that is one of theNAD+-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 mechanismof nicotinamidase Pnc1, we overexpressed, purified, and crystallized the N-terminally His6-tagged Pnc1 protein fromKluyveromyces 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= 90º. There is one moleculein the asymmetric unit.
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참고문헌 (17)
참고문헌 신청
Adams, P. D. / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr D Biol Crystallogr 66:213~221
Anderson, R. M. / 2002 / Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels / J Biol Chem 277:18881~18890
Belenky, P. / 2007 / NAD+ metabolism in health and disease / Trends Biochem Sci 32:12~19
Blander, G. / 2004 / The Sir2 family of protein deacetylases / Annu Rev Biochem 73:417~435
Chang, J. H. / 2002 / Structural basis for the NAD-dependent deacetylase mechanism of Sir2 / J Biol Chem 277:34489~34498
Anderson, R. M. / 2002 / Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels / J Biol Chem 277:18881~18890
Belenky, P. / 2007 / NAD+ metabolism in health and disease / Trends Biochem Sci 32:12~19
Blander, G. / 2004 / The Sir2 family of protein deacetylases / Annu Rev Biochem 73:417~435
Chang, J. H. / 2002 / Structural basis for the NAD-dependent deacetylase mechanism of Sir2 / J Biol Chem 277:34489~34498
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