Figure 1From: Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis Two parallel oxidoreductase systems are depicted for disulfide bond formation of Mtb secreted proteins. Mt-DsbD (Rv2874) and/or Rv2877c are predicted to maintain the redox states of Mt-DsbE (Rv2878c) and Mt-DsbF (Rv1677) while Mt-VKOR (Rv2968c) is proposed to maintain the redox state of its genomic neighbor, Mt-DsbA (Rv2969c).Back to article page