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Gene Review: 

ECs3084  -  DsbE

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs3084

  • Because Dsb proteins in Escherichia coli and other bacteria seem to catalyze proper folding during protein secretion and because folding of secreted proteins is thought to be coupled to disulfide oxidoreduction, the function of Mtb DsbE may be to ensure that secreted proteins are in their correctly folded states [1].
  • Mycobacterium tuberculosis, a Gram-positive bacterium, encodes a secreted Dsb-like protein annotated as Mtb DsbE (Rv2878c, also known as MPT53) [1].
  • Biochemical characterization of Mtb DsbE reveals that this disulfide oxidoreductase is an oxidant, unlike Gram-negative bacteria DsbE proteins, which have been shown to be weak reductants [1].
 

High impact information on ECs3084

  • In addition, the pK(a) value of the active site, solvent-exposed cysteine is approximately 2 pH units lower than that of Gram-negative DsbE homologs [1].
  • Reduction of non-native protein disulphides in the periplasm of Escherichia coli is catalysed by three enzymes, DsbC, DsbG and DsbE, each of which harbours a catalytic Cys-X-X-Cys dithiol motif [2].
  • The N-terminal domain of DsbD, DsbD(N), acts as a versatile adaptor in electron transport and is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD(C) [3].
 

Analytical, diagnostic and therapeutic context of ECs3084

References

  1. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. Goulding, C.W., Apostol, M.I., Gleiter, S., Parseghian, A., Bardwell, J., Gennaro, M., Eisenberg, D. J. Biol. Chem. (2004) [Pubmed]
  2. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Chung, J., Chen, T., Missiakas, D. Mol. Microbiol. (2000) [Pubmed]
  3. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Goulding, C.W., Sawaya, M.R., Parseghian, A., Lim, V., Eisenberg, D., Missiakas, D. Biochemistry (2002) [Pubmed]
  4. Crystallization and preliminary crystallographic studies of Escherichia coli CcmG/DsbE protein. Ouyang, N., Chen, W.Y., Li, Q., Gao, Y.G., Hu, H.Y., Xia, Z.X. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
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