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. Author manuscript; available in PMC: 2016 Aug 12.
Published in final edited form as: Mol Microbiol. 2015 Sep 25;98(6):1037–1050. doi: 10.1111/mmi.13172

Fig. 2.

Fig. 2

Structural analysis of the C. diphtheriae disulfide bond-forming protein MdbA.

A. The C. diphtheriae MdbA crystal structure (residues 43–244), solved to a 1.77-Å resolution, possesses a thioredoxin-like domain (rainbow colors) and an alpha-helical domain (light brown).

B. The MdbA active site is comprised of C91, P92, H93 and C94. The Sγ group in the two cysteine residues forms a hydrogen bond with S221 of the Cis-Pro element.

C–F. The MdbA structure (green) was aligned with M. tuberculosis DsbA (C; PDB: 4K6X), B. subtilis BdbB (D; PDB:3EU3), S. aureus DsbA (E; PDB:3BCI) and E. coli DsbA (F; PDB:1A2L).