Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.

ABSTRACT: Cupredoxins are copper-dependent electron-transfer proteins that can be categorized as blue, purple, green, and red depending on the spectroscopic properties of the Cu(II) bound forms. Interestingly, despite significantly different first coordination spheres and nuclearity, all cupredoxins share a common Greek Key β-sheet fold. We have previously reported the design of a red copper protein within a completely distinct three-helical bundle protein, α₃DChC2. (1) While this design demonstrated that a β-barrel fold was not requisite to recapitulate the properties of a native cupredoxin center, the parent peptide α₃D was not sufficiently stable to allow further study through additional mutations. Here we present the design of an elongated protein GRANDα₃D (GRα

SUBMITTER: Koebke KJ 

PROVIDER: S-EPMC6183058 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature