Fig. 3: Overall structure of SIRT3-H3K9bhb complex.
From: Molecular basis for hierarchical histone de-β-hydroxybutyrylation by SIRT3
a Ribbon view of SIRT3 (blue) bound to H36–15K9bhb peptide (yellow) with K9bhb highlighted as sticks. Gray ball, zinc ion of the zinc finger motif within SIRT3. Residues A7 to G13 of the H36–15K9bhb peptide are well traced as shown by the Fo-Fc omit map countered at 2.2 σ level. b The topology of SIRT3 catalytic domain. Magenta cylinders, α-helices; Cyan arrows, β-strands. Binding positions of zinc, H3K9bhb and NAD+ cofactor were annotated as gray circle, yellow and gray rectangles, respectively. c Conformational changes of SIRT3 upon H3K9bhb peptide binding. H3K9bhb-bound binary structure (blue) is superimposed with the apo form SIRT3 (pink, PDB: 3GLS). Note the 18.6° rotation of the small lobe as illustrated in the schematic diagram. d Electrostatic surface view of SIRT3 bound to H3K9bhb peptide depicted as space-filling spheres. Electrostatic potential is expressed as a spectrum ranging from −6 kT/e (red) to +6 kT/e (blue). A cutaway view of the Kbhb insertion pocket is highlighted in the close-up box. Note the extra space next to the tip of Kbhb
