Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate.

ABSTRACT: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the Cu_A protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba ₃ oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCu_A were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCu_A and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide intermediate. The cysteine of TtSco that attacks the disulfide bond in the target TtCu_A protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive

SUBMITTER: Lopez LC 

PROVIDER: S-EPMC6201729 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature