Structural Basis of a Thiol-Disulfide Oxidoreductase in the Hedgehog-Forming Actinobacterium Corynebacterium matruchotii.

ABSTRACT: The actinobacterium Corynebacterium matruchotii has been implicated in nucleation of oral microbial consortia leading to biofilm formation. Due to the lack of genetic tools, little is known about basic cellular processes, including protein secretion and folding, in this organism. We report here a survey of the C. matruchotii genome, which encodes a large number of exported proteins containing paired cysteine residues, and identified an oxidoreductase that is highly homologous to the Corynebacterium diphtheriae thiol-disulfide oxidoreductase MdbA (MdbA_Cd). Crystallization studies uncovered that the 1.2-Å resolution structure of C. matruchotii MdbA (MdbA_Cm) possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-

SUBMITTER: Luong TT 

PROVIDER: S-EPMC5892113 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature