Deciphering NAD-Dependent Deacetylases Robert N. Dutnall, Lorraine Pillus  Cell  Volume 105, Issue 2, Pages 161-164 (April 2001) DOI: 10.1016/S0092-8674(01)00305-1

Figure 1 The Conserved Core Domain in the Sir2p Family (a) Schematic representation of sequences of selected members of the Sir2p family of NAD-dependent deacetylases. Sequences shown illustrate the diversity in the lengths of N- and C-terminal regions outside of the conserved core domain. (b) Enlargement of Sir2-Af1 illustrating the contributions of sequence regions to the multidomain structure of the core domain. Numbers within the boxes represent the approximate length of the respective regions. Triangles indicate the approximate locations in which additional residues are inserted in other members of the Sir2p family (discussed in the text) Cell 2001 105, 161-164DOI: (10.1016/S0092-8674(01)00305-1)

Figure 2 Overview of the Sir2-Af1/NAD Complex Schematic representation of the Sir2-Af1/NAD complex structure. The zinc ion is shown as a gray sphere along with the locations of the coordinating cysteine residues. NAD is shown in a ball-and-stick representation; red, nicotinamide ring (inferred position); blue, adenine ring; purple, ribose and phosphate moieties. The approximate locations of sites A, B, and C of the NAD binding site are indicated. An open circle indicates the entrance to the channel through which an acetyl-lysine side chain could enter site B. The location of the substrate binding cleft proposed by Min et al. is indicated along with a possible alternative binding site in a shallow groove of the Rossmann fold domain (dashed line). Triangles indicate positions of sequence insertions (see Figure 1b) Cell 2001 105, 161-164DOI: (10.1016/S0092-8674(01)00305-1)