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. 2018 Aug 24;20:130–145. doi: 10.1016/j.redox.2018.08.017

Table 1.

The conserved targets for S-bacillithiolation and their available crystal structures.

Protein Organism Related structures (PDB ID) Cysteine residues Function of the cysteine residue Confirmed post-translational modificationa
AldA Staphylococcus aureus 3TY7 C279 active site residue S-bacillithiolation
GapDH Staphylococcus aureus 3LC7 C96 - -
3LVF C151 active site residue S-bacillithiolation, overoxidation
5T73
GuaB Staphylococcus aureus - C307 active site S-bacillithiolation
C326 - S-bacillithiolation
GuaB Bacillus anthracis 3TSB C308 active site S-bacillithiolation
3USB C327 - S-bacillithiolation
3TSD
MetE Staphylococcus aureus - C632 zinc-binding site -
C715 zinc-binding site S-bacillithiolation
MetE Streptococcus mutans 3L7R C632 zinc-binding site -
3T0C C715 zinc-binding site S-bacillithiolation
PpaC Staphylococcus aureus 4RPA C110 - overoxidation
C118 - -
C158 - S-bacillithiolation, overoxidation
SarZ Staphylococcus aureus 3HRM C13 redox-active S-bacillithiolation
3HSE
3HSR
a

Also if confirmed in other species.