Extended Data Fig. 3: (a) AlphaFold-predicted BDH1_MOUSE structure.

Crosslinked residues were indicated in yellow spheres, and crosslinks shown in red lines mean they were increased in TAC samples. (b) The pLDDT plot of the predicted BDH_mouse structure. (c) Alignment of apo (grey, PDB: 3OXO chain A) and substrate-bound (yellow, PDB: 3OXO chain E) monomers of porcine SCOT1. CoA is colored in magenta and bound to the active site. Lysine sidechains are shown in stick representation. Alignment depicts the structural differences between the dynamic C-terminal domain and the static N-terminal domain during substrate-binding. A close-up view specifies cross-linked lysines (K418 and K421). (d) Ketone-driven oxygen consumption rate (OCR) of mitochondria isolated from TAC and Sham hearts. Baseline OCR (State 1) was measured, followed by sequential injections of β-hydroxybutyrate/malate (State 2), ADP (State 3), Oligomycin (State 4μ), and FCCP (FCCPmax). N=6 animals, AVG+/-SEM, *denotes p<0.05 by unpaired, two-tailed Student’s t-test.