{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lopez LC"],"funding":["Division of Chemistry","Research Corporation for Science Advancement","Division of Undergraduate Education","Welch Foundation"],"pagination":["1942-1954"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6201729"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(11)"],"pubmed_abstract":["The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the Cu<sub>A</sub> protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba <sub>3</sub> oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCu<sub>A</sub> were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCu<sub>A</sub> 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<sub>A</sub> protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive "],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate."],"pmcid":["PMC6201729"],"funding_grant_id":["7693","S-STEM 1153796","W-0031","CHE-1726441","S‐STEM 1153796","W‐0031","CHE‐1726441"],"pubmed_authors":["McKinney JR","Mukhitov N","Hofman CR","Lopez LC","Piers AD","Hunsicker-Wang LM","Hamme CS","Euers L","Wadler E","Handley LD"],"additional_accession":[]},"is_claimable":false,"name":"Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate.","description":"The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the Cu<sub>A</sub> protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba <sub>3</sub> oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCu<sub>A</sub> were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCu<sub>A</sub> 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<sub>A</sub> protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive ","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Nov","modification":"2026-04-16T11:07:19.417Z","creation":"2019-11-07T08:01:52Z"},"accession":"S-EPMC6201729","cross_references":{"pubmed":["30168216"],"doi":["10.1002/pro.3502"]}}