The first structures of the Drosophila germline-specific thioredoxins Deadhead (Dhd) and thioredoxin T (TrxT), which present unusual properties with respect to canonical Trxs, are reported. Dhd is highly positively charged, which facilitates nonspecific DNA binding to promote chromatin remodeling. TrxT contains a C-terminal extension, which is mostly unstructured and highly flexible, that modulates the redox activity of the protein. These structures will facilitate the virtual screening of small-molecule ligands and protein partners.