Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis.

@article{Goulding2004GrampositiveDP,
  title={Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis.},
  author={Celia W Goulding and Marcin I. Apostol and Stefan Gleiter and Angineh Parseghian and James C. A. Bardwell and Marila L Gennaro and David Eisenberg},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 5},
  pages={
          3516-24
        }
}
Mycobacterium tuberculosis, a Gram-positive bacterium, encodes a secreted Dsb-like protein annotated as Mtb DsbE (Rv2878c, also known as MPT53). 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. We have determined the crystal… CONTINUE READING

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