Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase

@inproceedings{Christensen2016StructuralAB,
  title={Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase},
  author={Signe Christensen and Morten K. Gr{\o}ftehauge and Karl A. Byriel and Wilhelmina M Huston and Emily Jane Furlong and Bego{\~n}a Heras and Jennifer L. Martin and R{\'o}is{\'i}n M McMahon},
  booktitle={PloS one},
  year={2016}
}
The Gram negative bacteria Chlamydia trachomatis is an obligate intracellular human pathogen that can cause pelvic inflammatory disease, infertility and blinding trachoma. C. trachomatis encodes a homolog of the dithiol oxidoreductase DsbA. Bacterial DsbA proteins introduce disulfide bonds to folding proteins providing structural bracing for secreted virulence factors, consequently these proteins are potential targets for antimicrobial drugs. Despite sharing functional and structural… CONTINUE READING
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