The suppressor of copper sensitivity protein c from caulobacter crescentus is a trimeric disulfide isomerase that binds copper(i) with subpicomolar affinity

HIGHLIGHTS

  • who: X-ray crystallography et al. from the Griffith Institute for Drug Discovery, Griffith University, Don Young Road, Nathan, QLD, Australia, bCentre for have published the research: The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity, in the Journal: (JOURNAL)
  • what: The authors report the detailed functional and structural characterization of CcScsC. The authors show that CcScsC is a disulfide isomerase with an equivalent activity to that of EcDsbC (as is the C2S variant CcScsC used for crystal_structure determination), complements PmScsC in . . .

     

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