Crystal structure of DsbA from corynebacterium diphtheriae and its functional implications for CueP in gram-positive bacteria

Si Hyeon Um, Jin Sik Kim, Saemee Song, Nam Ah Kim, Seong Hoon Jeong, Nam Chul Ha

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

In Gram-negative bacteria in the periplasmic space, the dimeric thioredoxin-fold protein DsbC isomerizes and reduces incorrect disulfide bonds of unfolded proteins, while the monomeric thioredoxin-fold protein DsbA introduces disulfide bonds in folding proteins. In the Gram-negative bacteria Salmonella enterica serovar Typhimurium, the reduced form of CueP scavenges the production of hydroxyl radicals in the copper-mediated Fenton reaction, and DsbC is responsible for keeping CueP in the reduced, active form. Some DsbA proteins fulfill the functions of DsbCs, which are not present in Gram-positive bacteria. In this study, we identified a DsbA homologous protein (CdDsbA) in the Corynebacterium diphtheriae genome and determined its crystal structure in the reduced condition at 1.5 Å resolution. CdDsbA consists of a monomeric thioredoxin-like fold with an inserted helical domain and unique N-terminal extended region. We confirmed that CdDsbA has disulfide bond isomerase/reductase activity, and we present evidence that the N-terminal extended region is not required for this activity and folding of the core DsbA-like domain. Furthermore, we found that CdDsbA could reduce CueP from C. diphtheriae.

Original languageEnglish
Pages (from-to)715-722
Number of pages8
JournalMolecules and Cells
Volume38
Issue number8
DOIs
StatePublished - 17 Jun 2015

Keywords

  • CueP
  • Disulfide
  • DsbA
  • Gram-positive bacteria

Fingerprint

Dive into the research topics of 'Crystal structure of DsbA from corynebacterium diphtheriae and its functional implications for CueP in gram-positive bacteria'. Together they form a unique fingerprint.

Cite this