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Figure 4.
Figure 4. Structural comparison between SIRT2 and Sir2-Af1.
a, Superposition of SIRT2 Rossmann fold with Sir2-Af1 in stereo.
SIRT2 is shown in cyan and positioned approximately in the same
orientation as in Fig. 1 (right), and Sir2-Af1 is in gray. The
zinc from SIRT2 is in magenta, whereas the zinc atom from
Sir2-Af1 is in orange. The NAD molecule from the Sir2-Af1 -NAD
complex is in red. The SIRT2 small pocket and the L-1B loop of
Sir2-Af1 are labeled. Notice the increased size of the Sir2-Af1
acetyl-lysine binding site in SIRT2. b, A stereo, close-up view
of the NAD binding sites of SIRT2 and Sir2-Af1. The view shows
the molecules turned 90° along a horizontal axis in the plane of
the paper. Conserved SIRT2 residues that are candidates for
NAD-binding or catalysis are shown as ball-and-stick
representations and are labeled.
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