Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR026591
The catalytic core of sirtuin proteins consists of a large and a small domains. The large domain has a Rossmann fold and binds NAD+. The small domain is composed of residues from two insertions in the Rossmann fold that form a helical and a zinc binding modules
[1, 2]. This superfamily represents the catalytic core small domain.
References Imported from IPR026591
1.Crystal structure of a SIR2 homolog-NAD complex. Min J, Landry J, Sternglanz R, Xu RM. Cell 105, 269-79, (2001). View articlePMID: 11336676
2.Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Avalos JL, Celic I, Muhammad S, Cosgrove MS, Boeke JD, Wolberger C. Mol. Cell 10, 523-35, (2002). View articlePMID: 12408821