Supplementary Materials

This PDF file includes:

  • Fig. S1. Hydrogen bonds and disulfide bridges between chain A and chain B in WT AtFN3K.
  • Fig. S2. Oxidized monomeric species are an artifact of the SDS-PAGE gel.
  • Fig. S3. WT and triple cysteine mutant (C32A/C236A/C196A) AtFN3K exist as two distinct species.
  • Fig. S4. Reducing and nonreducing SDS-PAGE of dimer and monomer fractions of WT and triple cysteine mutant AtFN3K.
  • Fig. S5. Effects of thiol reagents on the activity of WT and cysteine mutant AtFN3K.
  • Fig. S6. P-loop cysteine (Cys24) is critical for the formation of disulfide-linked dimer in HsFN3K.
  • Fig. S7. Western blot of HsFN3K KO in HepG2 cells.
  • Fig. S8. WT and C32A/C236A AtFN3K localize to the nucleus.
  • Fig. S9. Multiple sequence alignment showing the conservation of P-loop cysteine in selected human ePKs and FN3Ks.
  • Fig. S10. FN3K and FN3KRP expression levels in human tumors.
  • Fig. S11. Spectral data of ribulose-N-α-Ac-lysine.
  • Table S1. Data collection and refinement statistics of WT AtFN3K.
  • Table S2. Metabolites identified in extracts of WT HepG2 and FN3K-KO cells.
  • References (88, 89)

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