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. 2023 Mar 10;24(5):e56052. doi: 10.15252/embr.202256052

Figure 4. Crystallographic studies of SIRT3 in complex with CCNE2K348la.

Figure 4

  1. The overall complex structure of SIRT3 (gray) interaction with CCNE2K348la peptide (green).
  2. The catalytic pocket of SIRT3 catalyzing the Kla group. Several residues (yellow) consist of the pocket to accommodate the Kla group, nearby Phe8 and two imidazole molecules (green).
  3. The structural superimposition of SIRT3/CCNE2Kla (green) with SIRT3/AceCS2Kac (PDB 3GLR, Cyan). The reconfiguration of the residues (D156, F157, R158) in the catalytic pocket facilitates the Kla group binding compared to those conformations when SIRT3 binds with Kac.
  4. A conformational change of the residue V324 facilitates the formation of a pocket together with F8 from CCNE2 peptide and re‐organizes F157 to accommodate two imidazoles bridging the interaction of SIRT3 with the peptide substrate.