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. Author manuscript; available in PMC: 2012 Nov 11.
Published in final edited form as: Science. 2011 Nov 11;334(6057):806–809. doi: 10.1126/science.1207861

Fig. 1.

Fig. 1

The structure of Sirt5 revealed an unusual acyl pocket. (A) The acyl pocket of Sirt5 was partially occupied by the sulfate from the CHES molecule via interactions with Arg105 and Tyr102. The sulfur was 4.2 Å away from the thioacetyl group. (B) Alignment of Sirt5-thioacetyl peptide structure (grey) and Sir2Tm-acetyl peptide structure (PDB 2h4f, magenta). (C) The rationale for predicting that malonyl/succinyl peptides could be better substrates for Sirt5. (D) Sirt5-succinyl peptide-NAD ternary structure showing that the succinyl group interacted with Tyr102 and Arg105.